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Volumn 107, Issue 96, 1999, Pages 5-46

Mammalian Cu-containing amine oxidases (CAOs): New methods of analysis, structural relationships, and possible functions

(1)  Houen, Gunnar a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; AMINE OXIDASE (COPPER CONTAINING); ORNITHINE; ORNITHINE DECARBOXYLASE; POLYAMINE; SINGLE STRANDED DNA; SPERMIDINE; SPERMINE;

EID: 0033256133     PISSN: 0903465X     EISSN: None     Source Type: Journal    
DOI: 10.1111/apm.1999.107.s96.5     Document Type: Review
Times cited : (33)

References (476)
  • 1
    • 0014373548 scopus 로고
    • Amine oxidase. XII. The association and dissociation, and number of subunits of beef plasma amine oxidase
    • Achee, F. M., Chervenka, C. H., Smith, R. A. and Yasunobu, K. T. (1968). Amine oxidase. XII. The association and dissociation, and number of subunits of beef plasma amine oxidase. Biochemistry 7, 4329-4335.
    • (1968) Biochemistry , vol.7 , pp. 4329-4335
    • Achee, F.M.1    Chervenka, C.H.2    Smith, R.A.3    Yasunobu, K.T.4
  • 2
    • 0027939558 scopus 로고
    • Heat enhancement of cytotoxicity induced by oxidation products of spermine in chinese hamster ovary cells
    • Agostinello, E., Przybytkowski, E., Mondovi, B. and Averill-Bates, D. A. (1994). Heat enhancement of cytotoxicity induced by oxidation products of spermine in chinese hamster ovary cells. Biochem. Pharmacol. 48, 1181-1186.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1181-1186
    • Agostinello, E.1    Przybytkowski, E.2    Mondovi, B.3    Averill-Bates, D.A.4
  • 3
    • 0029965516 scopus 로고    scopus 로고
    • Glucose, glutathione, and cellular response to spermine oxidation products
    • Agostinello, E., Przybytkowski, E. and Averill-Bates, D. A. (1996). Glucose, glutathione, and cellular response to spermine oxidation products. Free Rad. Biol. Med. 20, 649-656.
    • (1996) Free Rad. Biol. Med. , vol.20 , pp. 649-656
    • Agostinello, E.1    Przybytkowski, E.2    Averill-Bates, D.A.3
  • 4
    • 0343261238 scopus 로고
    • Studies on the histaminolytic power of plasma with special reference to pregnancy
    • Ahlmark, A. (1944). Studies on the histaminolytic power of plasma with special reference to pregnancy. Acta Physiol. Scand. 9, Suppl. 28, 1-107.
    • (1944) Acta Physiol. Scand. , vol.9 , Issue.SUPPL. 28 , pp. 1-107
    • Ahlmark, A.1
  • 5
    • 0019251693 scopus 로고
    • Polyamine metabolites and conjugates in man and higher animals: A review of the litterature
    • Aigner-Held, R. and Daves, G. D. (1980). Polyamine metabolites and conjugates in man and higher animals: A review of the litterature. Physiol. Chem. Phys. 12, 389-400.
    • (1980) Physiol. Chem. Phys. , vol.12 , pp. 389-400
    • Aigner-Held, R.1    Daves, G.D.2
  • 6
    • 0009736856 scopus 로고
    • Isolation of acrolein from incubated mixtures of spermine with calf serum and its effects on mammalian cells
    • Alarcon, R. A. (1964). Isolation of acrolein from incubated mixtures of spermine with calf serum and its effects on mammalian cells. Arch. Biochem. Biophys. 106, 240-242.
    • (1964) Arch. Biochem. Biophys. , vol.106 , pp. 240-242
    • Alarcon, R.A.1
  • 7
    • 0014765080 scopus 로고
    • Acrolein. IV. Evidence for the formation of the cytotoxic aldehyde acrolein from enzymatically oxidised spermidine
    • Alarcon, R. A. (1970). Acrolein. IV. Evidence for the formation of the cytotoxic aldehyde acrolein from enzymatically oxidised spermidine. Arch. Biochem. Biophys. 137, 365-372.
    • (1970) Arch. Biochem. Biophys. , vol.137 , pp. 365-372
    • Alarcon, R.A.1
  • 8
    • 0023253145 scopus 로고
    • Cadaverine supplementation during a chronic exposure to difluoromethylornithine allows an overexpression, but prevents gene amplification, of ornithine decarboxylase in L1210 mouse leukaemia cells
    • Alhonen-Hongistu, L., Hirvonen, A., Sinervirta, R. and Jänne, J. (1987). Cadaverine supplementation during a chronic exposure to difluoromethylornithine allows an overexpression, but prevents gene amplification, of ornithine decarboxylase in L1210 mouse leukaemia cells. Biochem. J. 247, 651-655.
    • (1987) Biochem. J. , vol.247 , pp. 651-655
    • Alhonen-Hongistu, L.1    Hirvonen, A.2    Sinervirta, R.3    Jänne, J.4
  • 9
    • 0020572638 scopus 로고
    • Stimulation of clonal tumor cell growth in vitro by inhibiting the serum polyamine oxidase activity
    • Ali-Osman, F. and Maurer, H. R. (1983). Stimulation of clonal tumor cell growth in vitro by inhibiting the serum polyamine oxidase activity. J. Cancer Res. Clin. Oncol. 106, 17-20.
    • (1983) J. Cancer Res. Clin. Oncol. , vol.106 , pp. 17-20
    • Ali-Osman, F.1    Maurer, H.R.2
  • 10
    • 0017776812 scopus 로고
    • Identification of a thymic inhibitor (chalone) of lymphocyte transformation as a spermine complex
    • Allen, J. C., Smith, C. J., Curry, M. C. and Gaugas, J. M. (1977). Identification of a thymic inhibitor (chalone) of lymphocyte transformation as a spermine complex. Nature 267, 623-625.
    • (1977) Nature , vol.267 , pp. 623-625
    • Allen, J.C.1    Smith, C.J.2    Curry, M.C.3    Gaugas, J.M.4
  • 11
    • 0018595176 scopus 로고
    • Inhibition of lymphocyte proliferation by polyamines requires ruminant-plasma polyamine oxidase
    • Allen, J. C., Smith, C. J., Hussain, J. I., Thomas, J. M. and Gaugas, J. M. (1979). Inhibition of lymphocyte proliferation by polyamines requires ruminant-plasma polyamine oxidase. Eur. J. Immunol. 102, 153-158.
    • (1979) Eur. J. Immunol. , vol.102 , pp. 153-158
    • Allen, J.C.1    Smith, C.J.2    Hussain, J.I.3    Thomas, J.M.4    Gaugas, J.M.5
  • 12
    • 0023093388 scopus 로고
    • Role of spermine in the cytotoxic effects of seminal plasma
    • Allen, R. D. and Roberts, T. K. (1987). Role of spermine in the cytotoxic effects of seminal plasma. Am. J. Reprod. Immunol. Microbiol. 13, 4-8.
    • (1987) Am. J. Reprod. Immunol. Microbiol. , vol.13 , pp. 4-8
    • Allen, R.D.1    Roberts, T.K.2
  • 13
    • 0023923582 scopus 로고
    • Participation of aldehyde dehydrogenase in the oxidative deamination pathway of histamine and putrescine
    • Ambroziak, W. and Maslinski, C. (1988). Participation of aldehyde dehydrogenase in the oxidative deamination pathway of histamine and putrescine. Agents and Actions. 23, 311-313
    • (1988) Agents and Actions. , vol.23 , pp. 311-313
    • Ambroziak, W.1    Maslinski, C.2
  • 14
    • 0021704210 scopus 로고
    • Rapid characterisation and partial purification of various animal amine oxidases
    • Amicosante, G., Oratore, A., Crifo, C. and Finazzi-Agro, A. (1984). Rapid characterisation and partial purification of various animal amine oxidases. Experientia 40, 1140-1142.
    • (1984) Experientia , vol.40 , pp. 1140-1142
    • Amicosante, G.1    Oratore, A.2    Crifo, C.3    Finazzi-Agro, A.4
  • 16
    • 0018387777 scopus 로고
    • The influence of some drugs on the determination of diamine oxidase activity
    • Andersson, A.-C., Henningson, S. and Rosengren, E. (1979). The influence of some drugs on the determination of diamine oxidase activity. Agents and Actions 9, 44.
    • (1979) Agents and Actions , vol.9 , pp. 44
    • Andersson, A.-C.1    Henningson, S.2    Rosengren, E.3
  • 17
    • 0020353885 scopus 로고
    • Characteristics of rat skull benzylamine oxidase
    • Andree, T. H. and Clarke, D. E. (1982). Characteristics of rat skull benzylamine oxidase. Proc. Soc. Exp. Biol. Med. 171, 298-305.
    • (1982) Proc. Soc. Exp. Biol. Med. , vol.171 , pp. 298-305
    • Andree, T.H.1    Clarke, D.E.2
  • 18
    • 84914647046 scopus 로고
    • The histaminolytic action of blood during pregnancy
    • Anrep, G. V., Barsoum, G. S. and Ibrahim, A. (1947). The histaminolytic action of blood during pregnancy. J. Physiol. 106, 379-393.
    • (1947) J. Physiol. , vol.106 , pp. 379-393
    • Anrep, G.V.1    Barsoum, G.S.2    Ibrahim, A.3
  • 19
    • 0030442943 scopus 로고    scopus 로고
    • Quinoprotein-catalysed reactions
    • Anthony, C. (1996). Quinoprotein-catalysed reactions. Biochem. J. 320, 697-711.
    • (1996) Biochem. J. , vol.320 , pp. 697-711
    • Anthony, C.1
  • 20
    • 0019776595 scopus 로고
    • Localization of diamine oxidase in pig kidney: Immunofluorescence method
    • Argento-Cerú, M. P., Oratore, A., Mondovi, B. and Finazzi-Agró, A. (1981a). Localization of diamine oxidase in pig kidney: Immunofluorescence method. Cell. Mol. Biol. 27, 359-362.
    • (1981) Cell. Mol. Biol. , vol.27 , pp. 359-362
    • Argento-Cerú, M.P.1    Oratore, A.2    Mondovi, B.3    Finazzi-Agró, A.4
  • 22
    • 0029923135 scopus 로고    scopus 로고
    • Lymphocyte binding to vascular endothelium in inflamed skin revisited: A central role for vascular adhesion protein-1 (VAP-1)
    • Arvilommi, A. M., Salmi, M., Kalimo, K. and Jalkanen, S. (1996). Lymphocyte binding to vascular endothelium in inflamed skin revisited: A central role for vascular adhesion protein-1 (VAP-1). Eur. J. Immunol. 26, 825-833.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 825-833
    • Arvilommi, A.M.1    Salmi, M.2    Kalimo, K.3    Jalkanen, S.4
  • 23
    • 0030858739 scopus 로고    scopus 로고
    • Organ-selective regulation of vascular adhesion protein-1 in man
    • Arvilommi, A. M., Salmi, M. and Jalkanen, S. (1997). Organ-selective regulation of vascular adhesion protein-1 in man. Eur. J. Immunol. 27, 1794-1800.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1794-1800
    • Arvilommi, A.M.1    Salmi, M.2    Jalkanen, S.3
  • 24
    • 0026683752 scopus 로고
    • Ornithine decarboxylase activity is critical for cell transformation
    • Auvinen, M., Paasinen, A., Anderson, L. C. and Hölttä, E. (1992). Ornithine decarboxylase activity is critical for cell transformation. Nature 360, 355-358.
    • (1992) Nature , vol.360 , pp. 355-358
    • Auvinen, M.1    Paasinen, A.2    Anderson, L.C.3    Hölttä, E.4
  • 25
    • 0027293584 scopus 로고
    • Cytotoxicity and kinetic analysis of purified bovine serum amine oxidase in the presence of spermine in Chinese hamster ovary cells
    • Averill-Bates, D. A., Agostinello, E., Przybytkowski, E., Mateescu, M. A. and Mondovi, B. (1993). Cytotoxicity and kinetic analysis of purified bovine serum amine oxidase in the presence of spermine in Chinese hamster ovary cells. Arch. Biochem. Biophys. 300, 75-79.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 75-79
    • Averill-Bates, D.A.1    Agostinello, E.2    Przybytkowski, E.3    Mateescu, M.A.4    Mondovi, B.5
  • 26
    • 0028189807 scopus 로고
    • Aldehyde dehydrogenase and cytotoxicity of purified bovine serum amine oxidase and spermine in Chinese hamster ovary cells
    • Averill-Bates, D. A., Agostinello, E., Przybytkowski, E. and Mondovi, B. (1994). Aldehyde dehydrogenase and cytotoxicity of purified bovine serum amine oxidase and spermine in Chinese hamster ovary cells. Biochem. Cell Biol. 72, 36-42.
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 36-42
    • Averill-Bates, D.A.1    Agostinello, E.2    Przybytkowski, E.3    Mondovi, B.4
  • 27
    • 0022914429 scopus 로고
    • Determination of amine oxidases in tissues by peroxidation-induced chemiluminescense of phthalazines
    • Avigliani, L., Rossi, A., Marcozzi, G. and Finazzi-Agró, A. (1986). Determination of amine oxidases in tissues by peroxidation-induced chemiluminescense of phthalazines. Anal. Biochem. 159, 67-72.
    • (1986) Anal. Biochem. , vol.159 , pp. 67-72
    • Avigliani, L.1    Rossi, A.2    Marcozzi, G.3    Finazzi-Agró, A.4
  • 29
    • 0343261236 scopus 로고
    • The formation of spermidine from spermine by serum amine oxidase
    • Bachrach, U. and Bar-Or, R. (1960). The formation of spermidine from spermine by serum amine oxidase. Biochim. Biophys. Acta 40, 545.
    • (1960) Biochim. Biophys. Acta , vol.40 , pp. 545
    • Bachrach, U.1    Bar-Or, R.2
  • 30
    • 0013937003 scopus 로고
    • Inhibitory effect of oxidised spermine on the multiplication of coliphage T5
    • Bachrach, U. and Leibovici, J. (1966). Inhibitory effect of oxidised spermine on the multiplication of coliphage T5. J. Mol. Biol. 19, 120-132.
    • (1966) J. Mol. Biol. , vol.19 , pp. 120-132
    • Bachrach, U.1    Leibovici, J.2
  • 31
    • 0012856360 scopus 로고
    • Cytotoxic effect of oxidised spermine on Ehrlich ascites cells
    • Bachrach, U., Abzug, S. and Bekierkunst, A. (1967). Cytotoxic effect of oxidised spermine on Ehrlich ascites cells. Biochim. Biophys. Acta 134, 174-181.
    • (1967) Biochim. Biophys. Acta , vol.134 , pp. 174-181
    • Bachrach, U.1    Abzug, S.2    Bekierkunst, A.3
  • 32
    • 0014218022 scopus 로고
    • Interaction of oxidized polyamines with DNA. I. Evidence for the formation of cross-links
    • Bachrach, U. and Eilon, G. (1967). Interaction of oxidized polyamines with DNA. I. Evidence for the formation of cross-links. Biochim. Biophys. Acta 145, 418-426.
    • (1967) Biochim. Biophys. Acta , vol.145 , pp. 418-426
    • Bachrach, U.1    Eilon, G.2
  • 33
    • 0014687523 scopus 로고
    • Interaction of oxidized polyamines with DNA. IV. Effect of DNA composition on the binding
    • Bachrach, U. and Eilon, G. (1969a). Interaction of oxidized polyamines with DNA. IV. Effect of DNA composition on the binding. Biochim. Biophys. Acta 179, 473-483.
    • (1969) Biochim. Biophys. Acta , vol.179 , pp. 473-483
    • Bachrach, U.1    Eilon, G.2
  • 34
    • 0014687551 scopus 로고
    • The effect of spermine and oxidized spermine on the enzymic degradation of DNA
    • Bachrach, U. and Eilon, G. (1969b). The effect of spermine and oxidized spermine on the enzymic degradation of DNA. Biochim. Biophys. Acta 179, 494-496.
    • (1969) Biochim. Biophys. Acta , vol.179 , pp. 494-496
    • Bachrach, U.1    Eilon, G.2
  • 35
    • 0014687519 scopus 로고
    • Interaction of oxidized polyamines with DNA. V. Inhibition of nucleic acid synthesis
    • Bachrach, U. and Persky, S. (1969). Interaction of oxidized polyamines with DNA. V. Inhibition of nucleic acid synthesis. Biochim. Biophys. Acta 179, 484-493.
    • (1969) Biochim. Biophys. Acta , vol.179 , pp. 484-493
    • Bachrach, U.1    Persky, S.2
  • 38
    • 0019222268 scopus 로고
    • Metabolism of polyamines by cultured gliomacells
    • Bachrach, U. (1980). Metabolism of polyamines by cultured gliomacells. Biochem. J. 188, 387-392.
    • (1980) Biochem. J. , vol.188 , pp. 387-392
    • Bachrach, U.1
  • 39
    • 0023256913 scopus 로고
    • Fusion-mediated microinjection of active amine and diamine oxidases into cultured cells: Effect on protein and DNA synthesis in chick embryo fibroblasts and in glioma cells
    • Bachrach, U., Ash, I., Abu-Elheiga, L., Hershkovitz, M. and Loyter, A. (1987a). Fusion-mediated microinjection of active amine and diamine oxidases into cultured cells: Effect on protein and DNA synthesis in chick embryo fibroblasts and in glioma cells. J. Cell. Physiol. 131, 92-98.
    • (1987) J. Cell. Physiol. , vol.131 , pp. 92-98
    • Bachrach, U.1    Ash, I.2    Abu-Elheiga, L.3    Hershkovitz, M.4    Loyter, A.5
  • 40
    • 0023119251 scopus 로고
    • Effect of microinjected amine and diamine oxidases on the ultrastructure of eucaryotic cultured cells
    • Bachrach, U., Ash, I. and Rahamim, E. (1987b). Effect of microinjected amine and diamine oxidases on the ultrastructure of eucaryotic cultured cells. Tissue and Cell 19, 39-50.
    • (1987) Tissue and Cell , vol.19 , pp. 39-50
    • Bachrach, U.1    Ash, I.2    Rahamim, E.3
  • 41
    • 0028587340 scopus 로고
    • Histamine degradative uptake by cultured human pulmonary vascular endothelial cells utilises an inflammatory cell diamine oxidase
    • Baenziger, N. L., Dalemar, L. R., Mack, P. and Haddock, R. C. (1994a). Histamine degradative uptake by cultured human pulmonary vascular endothelial cells utilises an inflammatory cell diamine oxidase. J. Biol. Chem. 269, 32858-32864.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32858-32864
    • Baenziger, N.L.1    Dalemar, L.R.2    Mack, P.3    Haddock, R.C.4
  • 42
    • 0028244208 scopus 로고
    • An environmentally regulated receptor for diamine oxidase modulates human endothelial cell/fibroblast histamine degradative uptake
    • Baenziger, N. L., Mack, P., Jong, Y.-J. I., Dalemar, L. R., Perez, N., Lindberg, C., Wilhelm, B. and Haddock, R. C. (1994b). An environmentally regulated receptor for diamine oxidase modulates human endothelial cell/fibroblast histamine degradative uptake. J. Biol. Chem. 269, 14892-14898.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14892-14898
    • Baenziger, N.L.1    Mack, P.2    Jong, Y.-J.I.3    Dalemar, L.R.4    Perez, N.5    Lindberg, C.6    Wilhelm, B.7    Haddock, R.C.8
  • 44
    • 0023680477 scopus 로고
    • On the presence of a clorgyline resistant benzylamine oxidase activity in mouse kidney
    • Banchelli, G., Buffoni, F. and Raimondi, L. (1988). On the presence of a clorgyline resistant benzylamine oxidase activity in mouse kidney. Pharmacol. Res. Commun. 20, 465-483.
    • (1988) Pharmacol. Res. Commun. , vol.20 , pp. 465-483
    • Banchelli, G.1    Buffoni, F.2    Raimondi, L.3
  • 45
    • 12644275745 scopus 로고    scopus 로고
    • Glutathione levels and sensitivity to apoptosis are regulated by changes in transaldolase expression
    • Banki, K., Hutter, E., Colombo, E., Gonchoroff, N. J. and Perl, A. (1996). Glutathione levels and sensitivity to apoptosis are regulated by changes in transaldolase expression. J. Biol. Chem. 271, 32994-33001.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32994-33001
    • Banki, K.1    Hutter, E.2    Colombo, E.3    Gonchoroff, N.J.4    Perl, A.5
  • 46
    • 0343261232 scopus 로고
    • In vitro stimulation of transcription by spermine and its interaction with rat liver genome
    • Barbiroli, B., Masotti, L., Moruzzi, M. S., Monti, M. G. and Moruzzi, G. (1978). In vitro stimulation of transcription by spermine and its interaction with rat liver genome. Adv. Polyam. Res. 1, 217-229.
    • (1978) Adv. Polyam. Res. , vol.1 , pp. 217-229
    • Barbiroli, B.1    Masotti, L.2    Moruzzi, M.S.3    Monti, M.G.4    Moruzzi, G.5
  • 49
    • 0014755980 scopus 로고
    • A reinvestigation of the substrate specificity of pig kidney diamine oxidase
    • Bardsley, W. G., Hill, C. M. and Lobley, R. W. (1970). A reinvestigation of the substrate specificity of pig kidney diamine oxidase. Biochem. J. 117, 169-176.
    • (1970) Biochem. J. , vol.117 , pp. 169-176
    • Bardsley, W.G.1    Hill, C.M.2    Lobley, R.W.3
  • 50
    • 0015980043 scopus 로고
    • The amine oxidases of human placenta and pregnancy serum
    • Bardsley, W. C., Crabbe, M. J. C. and Scott, I. V. (1974a). The amine oxidases of human placenta and pregnancy serum. Biochem. J. 139, 169-181.
    • (1974) Biochem. J. , vol.139 , pp. 169-181
    • Bardsley, W.C.1    Crabbe, M.J.C.2    Scott, I.V.3
  • 51
    • 0015980043 scopus 로고
    • The amine oxidases of human placenta and pregnancy serum
    • Bardstey, W. C., Crabbe, M. J. C. and Scott, I. V. (1974b). The amine oxidases of human placenta and pregnancy serum. Biochem. J. 139, 169-181.
    • (1974) Biochem. J. , vol.139 , pp. 169-181
    • Bardstey, W.C.1    Crabbe, M.J.C.2    Scott, I.V.3
  • 52
    • 0008624989 scopus 로고
    • β-Iminazolylethylamine a depressor constituent of intestinal mucosa
    • Barger, G. and Dale, H. H. (1910). β-Iminazolylethylamine a depressor constituent of intestinal mucosa. J. Physiol. 41, 499-503.
    • (1910) J. Physiol. , vol.41 , pp. 499-503
    • Barger, G.1    Dale, H.H.2
  • 53
    • 0018395462 scopus 로고
    • Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods
    • Barker, R., Boden, N., Cayley, G., Charlton, S. C., Henson, R., Holmes, M. C., Kelly, I. D. and Knowles, P. F. (1979). Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods. Biochem. J. 177, 289-302.
    • (1979) Biochem. J. , vol.177 , pp. 289-302
    • Barker, R.1    Boden, N.2    Cayley, G.3    Charlton, S.C.4    Henson, R.5    Holmes, M.C.6    Kelly, I.D.7    Knowles, P.F.8
  • 54
    • 0029102337 scopus 로고
    • An investigation of antioxidant status, DNA repair capacity and mutation as a function of age in humans
    • Barnett, Y. A. and King, C. M. (1995). An investigation of antioxidant status, DNA repair capacity and mutation as a function of age in humans. Matation Res. 338, 115-128.
    • (1995) Matation Res. , vol.338 , pp. 115-128
    • Barnett, Y.A.1    King, C.M.2
  • 55
    • 0021228148 scopus 로고
    • Amine oxidase activities in brown adipose tissue of the rat: Identification of semicarbazide-sensitive (clorgyline-resistant) activity at the fat cell membrane
    • Barrand, M. A. and Fox, S. A. (1984). Amine oxidase activities in brown adipose tissue of the rat: identification of semicarbazide-sensitive (clorgyline-resistant) activity at the fat cell membrane. J. Pharm. Pharmacol. 36, 652-658.
    • (1984) J. Pharm. Pharmacol. , vol.36 , pp. 652-658
    • Barrand, M.A.1    Fox, S.A.2
  • 56
    • 0023230920 scopus 로고
    • The interaction of spermine and pentamines with DNA
    • Basu, H. S. and Marton, L. J. (1987). The interaction of spermine and pentamines with DNA. Biochem. J. 244, 243-246.
    • (1987) Biochem. J. , vol.244 , pp. 243-246
    • Basu, H.S.1    Marton, L.J.2
  • 57
    • 0016704838 scopus 로고
    • Purification of histaminase (diamine oxidase) from human pregnancy plasma by affinity chromatography
    • Baylin, S. B. and Margolis, S. (1975). Purification of histaminase (diamine oxidase) from human pregnancy plasma by affinity chromatography. Biochim. Biophys. Acta 397, 294-306.
    • (1975) Biochim. Biophys. Acta , vol.397 , pp. 294-306
    • Baylin, S.B.1    Margolis, S.2
  • 58
    • 0018144760 scopus 로고
    • Association of diamine oxidase and ornithine decarboxylase with maturing cells in rapidly proliferating epithelium
    • Baylin, S. B., Stevens, S. A. and Shakir, K. M. M. (1978). Association of diamine oxidase and ornithine decarboxylase with maturing cells in rapidly proliferating epithelium. Biochim. Biophys. Acta 541, 415-419.
    • (1978) Biochim. Biophys. Acta , vol.541 , pp. 415-419
    • Baylin, S.B.1    Stevens, S.A.2    Shakir, K.M.M.3
  • 59
    • 0016767287 scopus 로고
    • Changes in plasma histaminase activity during normal early human pregnancy and pregnancy disorders
    • Beaven, M. A., Marshall, J. R., Baylin, S. B. and Sjoerdsma, A. (1975). Changes in plasma histaminase activity during normal early human pregnancy and pregnancy disorders. Am. J. Obstet. Gynecol. 123, 605-609.
    • (1975) Am. J. Obstet. Gynecol. , vol.123 , pp. 605-609
    • Beaven, M.A.1    Marshall, J.R.2    Baylin, S.B.3    Sjoerdsma, A.4
  • 60
    • 0342826396 scopus 로고
    • The metabolism of histamine by guinea-pig and rat lung in vitro
    • Bennett, A. (1965). The metabolism of histamine by guinea-pig and rat lung in vitro. Brit. J. Pharmacol. 24, 147-155.
    • (1965) Brit. J. Pharmacol. , vol.24 , pp. 147-155
    • Bennett, A.1
  • 62
    • 0000997597 scopus 로고
    • Occurrence of an amine oxidase in horse serum
    • Bergeret, B., Blaschko, H. and Hawes, R. (1957). Occurrence of an amine oxidase in horse serum. Nature 180, 1127-1128.
    • (1957) Nature , vol.180 , pp. 1127-1128
    • Bergeret, B.1    Blaschko, H.2    Hawes, R.3
  • 63
    • 0028278638 scopus 로고
    • The functional role of monoamine oxidases a and b in the mammalian central nervous system
    • Berry, M. D., Juorio, A. V. and Paterson, I. A. (1994). The functional role of monoamine oxidases A and B in the mammalian central nervous system. Progr. Neurobiol. 42, 375-391.
    • (1994) Progr. Neurobiol. , vol.42 , pp. 375-391
    • Berry, M.D.1    Juorio, A.V.2    Paterson, I.A.3
  • 64
    • 0006544784 scopus 로고
    • The disappearance of histamine from autolysing lung tissue
    • Best, C. H. (1929). The disappearance of histamine from autolysing lung tissue. J. Physiol. 67, 256-263.
    • (1929) J. Physiol. , vol.67 , pp. 256-263
    • Best, C.H.1
  • 65
    • 0013558190 scopus 로고
    • The inactivation of histamine
    • Best, C. H. and McHenry, E. W. (1930). The inactivation of histamine. J. Physiol. 70, 349-372.
    • (1930) J. Physiol. , vol.70 , pp. 349-372
    • Best, C.H.1    McHenry, E.W.2
  • 66
    • 0017337747 scopus 로고
    • Determination of histaminase (diamine oxidase) activity by o-dianisidine test: Interference of ceruloplasmin
    • Bieganski, T., Blasinska, M. Z. and Kusche, J. (1977). Determination of histaminase (diamine oxidase) activity by o-dianisidine test: Interference of ceruloplasmin. Agents and Actions 7, 85-92.
    • (1977) Agents and Actions , vol.7 , pp. 85-92
    • Bieganski, T.1    Blasinska, M.Z.2    Kusche, J.3
  • 67
    • 0020668834 scopus 로고
    • Biochemical, physiological and pathophysiological aspects of intestinal diamine oxidase
    • Bieganski, T. (1983). Biochemical, physiological and pathophysiological aspects of intestinal diamine oxidase. Acta Physiol. Pol. 34, 139-154.
    • (1983) Acta Physiol. Pol. , vol.34 , pp. 139-154
    • Bieganski, T.1
  • 69
    • 0021939965 scopus 로고
    • Activation of mammalian RNA polymerases by polyamines
    • Blair, D. G. R. (1985). Activation of mammalian RNA polymerases by polyamines. Int. J. Biochem. 17, 23-30.
    • (1985) Int. J. Biochem. , vol.17 , pp. 23-30
    • Blair, D.G.R.1
  • 71
    • 0342391662 scopus 로고
    • Enzymic oxidation of aliphatic diamines
    • Blaschko, H. and Hawkins, J. (1950). Enzymic oxidation of aliphatic diamines. Brit. J. Pharmacol. 5, 625-632.
    • (1950) Brit. J. Pharmacol. , vol.5 , pp. 625-632
    • Blaschko, H.1    Hawkins, J.2
  • 72
    • 0041333378 scopus 로고
    • Observations on spermine oxidase of mammalian plasma
    • Blaschko, H. and Hawes, R. (1959). Observations on spermine oxidase of mammalian plasma. J. Physiol. 145, 124-131.
    • (1959) J. Physiol. , vol.145 , pp. 124-131
    • Blaschko, H.1    Hawes, R.2
  • 74
    • 84916867337 scopus 로고
    • Primary and secondary amines as substrates of amine oxidases
    • Blaschko, H. (1960). Primary and secondary amines as substrates of amine oxidases. J. Physiol. 153, 17-18P.
    • (1960) J. Physiol. , vol.153
    • Blaschko, H.1
  • 75
    • 0342826394 scopus 로고
    • Spermine oxidase and benzylamine oxidase. Distribution, development and substrate specificity
    • Blaschko, H. and Bonney, R. (1962). Spermine oxidase and benzylamine oxidase. Distribution, development and substrate specificity. Proc. Roy. Soc. Ser. B 156, 268-279.
    • (1962) Proc. Roy. Soc. Ser. B , vol.156 , pp. 268-279
    • Blaschko, H.1    Bonney, R.2
  • 76
    • 0343261226 scopus 로고
    • Amine oxidase
    • (Ed. Boyer, P. D.), Academic Press, New York
    • Blaschko, H. (1963). Amine oxidase. In "The enzymes" 8 (Ed. Boyer, P. D.), pp. 337-351, Academic Press, New York.
    • (1963) The Enzymes , vol.8 , pp. 337-351
    • Blaschko, H.1
  • 77
    • 0025655814 scopus 로고
    • Semicarbazide-sensitive amine oxidase activity in rat aortic cultured smooth muscle cells
    • Blicharski, J. R. D. and Lyles, G. A. (1990). Semicarbazide-sensitive amine oxidase activity in rat aortic cultured smooth muscle cells. J. Neural. Transm. 32, 337-339.
    • (1990) J. Neural. Transm. , vol.32 , pp. 337-339
    • Blicharski, J.R.D.1    Lyles, G.A.2
  • 78
    • 0021149456 scopus 로고
    • H1 histone, polylysine and spermine facilitate nucleosome assembly in vitro
    • Bogdanova, E. S. (1984). H1 histone, polylysine and spermine facilitate nucleosome assembly in vitro. FEBS Lett. 175, 321-324.
    • (1984) FEBS Lett. , vol.175 , pp. 321-324
    • Bogdanova, E.S.1
  • 79
    • 0019403885 scopus 로고
    • Acetylderivatives as intermediates in polyamine catabolism
    • Bolkenius, F. N. and Seiler, N. (1981). Acetylderivatives as intermediates in polyamine catabolism. Int. J. Biochem. 13, 287-292.
    • (1981) Int. J. Biochem. , vol.13 , pp. 287-292
    • Bolkenius, F.N.1    Seiler, N.2
  • 80
    • 0021957073 scopus 로고
    • Specific inhibition of polyamine oxidase in vivo is a method for the elucidation of its physiological role
    • Bolkenius, F. N., Bey, P. and Seiler, N. (1985). Specific inhibition of polyamine oxidase in vivo is a method for the elucidation of its physiological role. Biochim. Biophys. Acta 838, 69-76.
    • (1985) Biochim. Biophys. Acta , vol.838 , pp. 69-76
    • Bolkenius, F.N.1    Bey, P.2    Seiler, N.3
  • 81
    • 0023659975 scopus 로고
    • The role of polyamine reutilisation in depletion of cellular stores of polyamines in non-proliferating tissues
    • Bolkenius, F. N. and Seiler, N. (1987). The role of polyamine reutilisation in depletion of cellular stores of polyamines in non-proliferating tissues. Biochim. Biophys. Acta 923, 125-135.
    • (1987) Biochim. Biophys. Acta , vol.923 , pp. 125-135
    • Bolkenius, F.N.1    Seiler, N.2
  • 82
    • 0032101975 scopus 로고    scopus 로고
    • Cloning and characterisation of mouse vascular adhesion protein-1 reveals a novel molecule with enzymatic activity
    • Bono, P., Salmi, M., Smith, D. J. and Jalkanen, S. (1998). Cloning and characterisation of mouse vascular adhesion protein-1 reveals a novel molecule with enzymatic activity. J. Immunol. 160, 5563-5571.
    • (1998) J. Immunol. , vol.160 , pp. 5563-5571
    • Bono, P.1    Salmi, M.2    Smith, D.J.3    Jalkanen, S.4
  • 83
    • 0024295013 scopus 로고
    • 1H NMR study of the base-pairing reactions of d(GGAATTCC): Salt and polyamine effects on the imino proton exchange
    • 1H NMR study of the base-pairing reactions of d(GGAATTCC): salt and polyamine effects on the imino proton exchange. Biochem. 27, 1184-1191.
    • (1988) Biochem. , vol.27 , pp. 1184-1191
    • Braunlin, W.H.1    Bloomfield, V.A.2
  • 85
    • 0025088773 scopus 로고
    • Spermine toxicity and glutathione depletion in BHK-21/C13 cells
    • Brunton, V. G., Grant, M. H. and Wallace, H. M. (1990). Spermine toxicity and glutathione depletion in BHK-21/C13 cells. Biochem. Pharmacol. 40, 1893-1900.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 1893-1900
    • Brunton, V.G.1    Grant, M.H.2    Wallace, H.M.3
  • 86
    • 0026076137 scopus 로고
    • Mechanisms of spermine toxicity in baby-hamster kidney (BHK) cells
    • Brunton, V. G., Grant, M. H. and Wallace, H. M. (1991). Mechanisms of spermine toxicity in baby-hamster kidney (BHK) cells. Biochem. J. 280, 193-198.
    • (1991) Biochem. J. , vol.280 , pp. 193-198
    • Brunton, V.G.1    Grant, M.H.2    Wallace, H.M.3
  • 87
    • 0030029335 scopus 로고    scopus 로고
    • In situ detection of diamine oxidase activity using enhanced chemiluminescence
    • Bruun, L. and Houen, G. (1996). In situ detection of diamine oxidase activity using enhanced chemiluminescence. Anal. Biochem. 233, 130-136.
    • (1996) Anal. Biochem. , vol.233 , pp. 130-136
    • Bruun, L.1    Houen, G.2
  • 88
    • 0032112201 scopus 로고    scopus 로고
    • Polyamine-stimulated binding of diamine oxidase to DNA
    • Bruun, L., Høgdall, E. V. S., Vuust, J. and Houen, G. (1998). Polyamine-stimulated binding of diamine oxidase to DNA. Acta Chem. Scand. 52, 921-929.
    • (1998) Acta Chem. Scand. , vol.52 , pp. 921-929
    • Bruun, L.1    Høgdall, E.V.S.2    Vuust, J.3    Houen, G.4
  • 89
    • 76549145151 scopus 로고
    • Benzylamine oxidase and histaminase: Purification and crystallization of an enzyme from pig plasma
    • Buffoni, F. and Blaschko, H. (1964). Benzylamine oxidase and histaminase: purification and crystallization of an enzyme from pig plasma. Proc. Roy. Soc. B 161, 153-167.
    • (1964) Proc. Roy. Soc. B , vol.161 , pp. 153-167
    • Buffoni, F.1    Blaschko, H.2
  • 90
    • 0013979088 scopus 로고
    • Histaminase and related amine oxidases
    • Buffoni, F. (1966). Histaminase and related amine oxidases. Pharmacol. Rev. 18, 1163-1199.
    • (1966) Pharmacol. Rev. , vol.18 , pp. 1163-1199
    • Buffoni, F.1
  • 91
    • 0014242243 scopus 로고
    • The nature of copper in pig plasma benzylamine oxidase
    • Buffoni, F., Corte, L. D., Knowles, P. F. (1968). The nature of copper in pig plasma benzylamine oxidase. Biochem. J. 106, 575-576.
    • (1968) Biochem. J. , vol.106 , pp. 575-576
    • Buffoni, F.1    Corte, L.D.2    Knowles, P.F.3
  • 92
    • 0016731851 scopus 로고
    • Histamine as inhibitor of pig aorta amine oxidase
    • Buffoni, F., Pirisino, R. and Marino, P. (1975). Histamine as inhibitor of pig aorta amine oxidase. Agents and Actions 5, 429-430.
    • (1975) Agents and Actions , vol.5 , pp. 429-430
    • Buffoni, F.1    Pirisino, R.2    Marino, P.3
  • 93
    • 0017338748 scopus 로고
    • Immunofluorescense histochemistry of porcine tissues using antibodies to pig plasma amine oxidase
    • Buffoni, F. and Corte, L. D. (1977). Immunofluorescense histochemistry of porcine tissues using antibodies to pig plasma amine oxidase. Proc. Roy. Soc. Lond. B. 195, 417-423.
    • (1977) Proc. Roy. Soc. Lond. B. , vol.195 , pp. 417-423
    • Buffoni, F.1    Corte, L.D.2
  • 94
    • 0029394936 scopus 로고
    • Hydrogen peroxide and the proliferation of BHK-21 cells
    • Burdon, R. H., Alliangana, D. and Gill, V. (1995). Hydrogen peroxide and the proliferation of BHK-21 cells. Free. Rad. Res. 23, 471-486.
    • (1995) Free. Rad. Res. , vol.23 , pp. 471-486
    • Burdon, R.H.1    Alliangana, D.2    Gill, V.3
  • 95
    • 0017776797 scopus 로고
    • Synthetic polyamines added to cultures containing bovine sera reversibly inhibit in vitro parameters of immunity
    • Byrd, W. J., Jacobs, D. M. and Amoss, M. S. (1977). Synthetic polyamines added to cultures containing bovine sera reversibly inhibit in vitro parameters of immunity. Nature 267, 621-623.
    • (1977) Nature , vol.267 , pp. 621-623
    • Byrd, W.J.1    Jacobs, D.M.2    Amoss, M.S.3
  • 96
    • 0023762103 scopus 로고
    • The role of histamine in the cardiovascular system
    • Cabanie, M. and Godfraind, T. (1988). The role of histamine in the cardiovascular system. Drugs Exp. Clin. Res. 19, 141-147.
    • (1988) Drugs Exp. Clin. Res. , vol.19 , pp. 141-147
    • Cabanie, M.1    Godfraind, T.2
  • 97
    • 0027385504 scopus 로고
    • Peroxisomes and peroxisomal enzymes along the crypt-villus axis of the rat intestine
    • Cablé, S., Kedinger, M. and Dauca, M. (1993). Peroxisomes and peroxisomal enzymes along the crypt-villus axis of the rat intestine. Differentiation 54, 99-108.
    • (1993) Differentiation , vol.54 , pp. 99-108
    • Cablé, S.1    Kedinger, M.2    Dauca, M.3
  • 98
    • 0028605705 scopus 로고
    • Evidence for a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase
    • Cai, D. and Klinman, J. P. (1994). Evidence for a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase. J. Biol. Chem. 269, 32039-32042.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32039-32042
    • Cai, D.1    Klinman, J.P.2
  • 99
    • 0021148312 scopus 로고
    • Polyamine metabolism in differentiating friend erythroleukemia cells
    • Canellakis, Z. N., Marsh, L. L., Young, P. and Bondy, P. K. (1984). Polyamine metabolism in differentiating Friend erythroleukemia cells. Cancer Res. 44, 3841-3845.
    • (1984) Cancer Res. , vol.44 , pp. 3841-3845
    • Canellakis, Z.N.1    Marsh, L.L.2    Young, P.3    Bondy, P.K.4
  • 100
    • 0021907935 scopus 로고
    • Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth
    • Canellakis, E. S., Kyriakidis, D. A., Rinehart Jr., C. A., Huang, S.-C, Panagiotides, C. and Fong, W.-F. (1985). Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth. Biosci. Rep. 5, 189-204.
    • (1985) Biosci. Rep. , vol.5 , pp. 189-204
    • Canellakis, E.S.1    Kyriakidis, D.A.2    Rinehart C.A., Jr.3    Huang, S.-C.4    Panagiotides, C.5    Fong, W.-F.6
  • 101
    • 0343261224 scopus 로고
    • On the sources of the histaminase present in thoracic duct lymph
    • Carlsten, A. (1950a). On the sources of the histaminase present in thoracic duct lymph. Acta Physiol. Scand. 20, Suppl. 70, 5-26.
    • (1950) Acta Physiol. Scand. , vol.20 , Issue.SUPPL. 70 , pp. 5-26
    • Carlsten, A.1
  • 102
    • 0342826393 scopus 로고
    • No change in histaminase content of lymph and plasma in cats during pregnancy
    • Carlsten, A. (1950b). No change in histaminase content of lymph and plasma in cats during pregnancy. Acta Physiol. Scand. 20, Suppl. 70, 27-31.
    • (1950) Acta Physiol. Scand. , vol.20 , Issue.SUPPL. 70 , pp. 27-31
    • Carlsten, A.1
  • 103
    • 0027946931 scopus 로고
    • Purification and active-site characterisation of equine plasma amine oxidase
    • Carter, S. R., McGuirl, M. A., Brown, D. E. and Dooley, D. M. (1994). Purification and active-site characterisation of equine plasma amine oxidase. J. Inorg. Biochem. 56, 127-141.
    • (1994) J. Inorg. Biochem. , vol.56 , pp. 127-141
    • Carter, S.R.1    McGuirl, M.A.2    Brown, D.E.3    Dooley, D.M.4
  • 104
    • 0023880427 scopus 로고
    • Effect of polyamine depletion on c-myc expression in human colon carcinoma cells
    • Celano, P., Baylin, S. B., Giardello, F. M., Nelkin, B. D. and Casero, R. A. (1988). Effect of polyamine depletion on c-myc expression in human colon carcinoma cells. J. Biol. Chem. 263, 5491-5494.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5491-5494
    • Celano, P.1    Baylin, S.B.2    Giardello, F.M.3    Nelkin, B.D.4    Casero, R.A.5
  • 105
    • 0024362217 scopus 로고
    • Polyamines differentially modulate the transcription of growth-associated genes in human colon carcinoma cells
    • Celano, P., Baylin, S. B., and Casero, R. A. (1989). Polyamines differentially modulate the transcription of growth-associated genes in human colon carcinoma cells. J. Biol. Chem. 264, 8922-8927.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8922-8927
    • Celano, P.1    Baylin, S.B.2    Casero, R.A.3
  • 106
    • 0024209430 scopus 로고
    • Resumption of cell cycle in Balb/c-3T3 fibroblasts arrested by polyamine depletion: Relation with "competence" gene expression
    • Charollais, R. H. and Mester, J. (1988). Resumption of cell cycle in Balb/c-3T3 fibroblasts arrested by polyamine depletion: relation with "competence" gene expression. J. Cell. Physiol. 137, 559-564.
    • (1988) J. Cell. Physiol. , vol.137 , pp. 559-564
    • Charollais, R.H.1    Mester, J.2
  • 107
    • 0028241890 scopus 로고
    • The human gene for diamine oxidase, an amilorid binding protein
    • Chassande, O., Renard, S., Barbry, P. and Lazdunski, M. (1994). The human gene for diamine oxidase, an amilorid binding protein. J. Biol. Chem. 269, 14484-14489.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14484-14489
    • Chassande, O.1    Renard, S.2    Barbry, P.3    Lazdunski, M.4
  • 108
    • 0021835728 scopus 로고
    • Excretion of polyamines by humans following inhibition of diamine oxidase
    • Chayen, R., Goldberg, S. and Burke, M. (1985). Excretion of polyamines by humans following inhibition of diamine oxidase. Israel J. Med. Sci. 21, 543-545.
    • (1985) Israel J. Med. Sci. , vol.21 , pp. 543-545
    • Chayen, R.1    Goldberg, S.2    Burke, M.3
  • 109
    • 0022611461 scopus 로고
    • Age dependency of the metabolic conversion of polyamines into amino acids in IMR-90 human embryonic lung diploid fibroblasts
    • Chen, K. Y. and Chang, Z.-F. (1986). Age dependency of the metabolic conversion of polyamines into amino acids in IMR-90 human embryonic lung diploid fibroblasts. J. Cell. Physiol. 128, 27-32.
    • (1986) J. Cell. Physiol. , vol.128 , pp. 27-32
    • Chen, K.Y.1    Chang, Z.-F.2
  • 110
    • 0020065421 scopus 로고
    • A comparison of cardiac and vascular clorgyline-resistant amine oxidase and monoamine oxidase
    • Clarke, D. E., Lyles, G. A. and Callingham, B. A. (1982). A comparison of cardiac and vascular clorgyline-resistant amine oxidase and monoamine oxidase. Biochem. Pharmacol. 31, 27-35.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 27-35
    • Clarke, D.E.1    Lyles, G.A.2    Callingham, B.A.3
  • 112
    • 0025073054 scopus 로고
    • Expression of gene rrg is associated with reversion of NTH 3T3 transformed by LTR-c-H-ras
    • Contente, S., Kenyon, K., Rimoldi, D. and Friedman, R. M. (1990). Expression of gene rrg is associated with reversion of NTH 3T3 transformed by LTR-c-H-ras. Science 249, 796-798.
    • (1990) Science , vol.249 , pp. 796-798
    • Contente, S.1    Kenyon, K.2    Rimoldi, D.3    Friedman, R.M.4
  • 115
    • 0021267452 scopus 로고
    • Diamine oxidase in rat small bowel: Distribution in different segments and cellular location
    • D'Agostino, L., D'Argentino, G., Ciacci, C., Daniele, B., Macchia, V. and Mazzacca, G (1984). Diamine oxidase in rat small bowel: Distribution in different segments and cellular location. Enzyme 31, 217-220.
    • (1984) Enzyme , vol.31 , pp. 217-220
    • D'Agostino, L.1    D'Argentino, G.2    Ciacci, C.3    Daniele, B.4    Macchia, V.5    Mazzacca, G.6
  • 117
  • 119
    • 0028049130 scopus 로고
    • 1-acetyltransferase in growing yoshida AH-130 hepatoma cells
    • 1-acetyltransferase in growing Yoshida AH-130 hepatoma cells. Hepatology 19, 728-734.
    • (1994) Hepatology , vol.19 , pp. 728-734
    • Desiderio, M.A.1    Bardella, L.2
  • 120
    • 0343261222 scopus 로고
    • Melanocytes, chalones and polyamines
    • (Ed. Gaugas, J. M.), Wiley and Sons, New York
    • Dewey, D. L. (1980). Melanocytes, chalones and polyamines. In Polyamines in biomedical research (Ed. Gaugas, J. M.), pp. 309-320, Wiley and Sons, New York.
    • (1980) Polyamines in Biomedical Research , pp. 309-320
    • Dewey, D.L.1
  • 121
    • 0028794538 scopus 로고
    • Determination of semicarbazide-sensitive amine oxidase activity in human plasma by high performance liquid chromatography with fluorimetric detection
    • Dijk, J. v., Boomsma, F., Alberts, G., Man in 't Veld, A. J. and Schalekamp, M. A. D. H. (1995). Determination of semicarbazide-sensitive amine oxidase activity in human plasma by high performance liquid chromatography with fluorimetric detection. J. Chr. B 663, 43-50.
    • (1995) J. Chr. B , vol.663 , pp. 43-50
    • Dijk, J.V.1    Boomsma, F.2    Alberts, G.3    Man In 't Veld, A.J.4    Schalekamp, M.A.D.H.5
  • 122
    • 0028054240 scopus 로고
    • Retinoic acid prevents downregulation of RAS recision gene/lysyl oxidase early in adipocyte differentiation
    • Dimaculangan, D. D., Chawla, A., Boak, A., Kagan, H. M. and Lazar, M. A. (1994). Retinoic acid prevents downregulation of RAS recision gene/lysyl oxidase early in adipocyte differentiation. Differentiation 58, 47-52.
    • (1994) Differentiation , vol.58 , pp. 47-52
    • Dimaculangan, D.D.1    Chawla, A.2    Boak, A.3    Kagan, H.M.4    Lazar, M.A.5
  • 123
    • 0025941497 scopus 로고
    • Cultured hepatocytes bind and internalize bovine serum amine oxidase-gold complexes
    • Dini, L., Agostinello, E. and Mondovi, B. (1991). Cultured hepatocytes bind and internalize bovine serum amine oxidase-gold complexes. Biochem. Biophys. Res. Commun. 179, 1169-1174.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 1169-1174
    • Dini, L.1    Agostinello, E.2    Mondovi, B.3
  • 124
    • 0030009040 scopus 로고    scopus 로고
    • Rapid and specific efflux of reduced glutathione during apoptosis induced by anti-fas/APO-1 antibody
    • Dobbelsteen, D. J., Nobel, C. S. I., Schlegel, J., Cotgreave, I. A., Orrenius, S. and Slater, A. F. G. (1996). Rapid and specific efflux of reduced glutathione during apoptosis induced by anti-fas/APO-1 antibody. J. Biol. Chem. 271, 15420-15427.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15420-15427
    • Dobbelsteen, D.J.1    Nobel, C.S.I.2    Schlegel, J.3    Cotgreave, I.A.4    Orrenius, S.5    Slater, A.F.G.6
  • 125
    • 0342826390 scopus 로고
    • A test for pregnancy based on the histaminolytic activity of serum
    • Dodge, A. C. (1952). A test for pregnancy based on the histaminolytic activity of serum. Am. J. Obst. Gynecol. 63, 1213-1222.
    • (1952) Am. J. Obst. Gynecol. , vol.63 , pp. 1213-1222
    • Dodge, A.C.1
  • 127
    • 84982059868 scopus 로고
    • Über den enzymatischen abbau des histamins I
    • Edlbacher, S. and Zeller, A. (1937). Über den enzymatischen Abbau des Histamins I. Helv. Chim. Acta 20, 717-726.
    • (1937) Helv. Chim. Acta , vol.20 , pp. 717-726
    • Edlbacher, S.1    Zeller, A.2
  • 128
    • 0019304134 scopus 로고
    • Molecular properties of the monoamine oxidases
    • Edwards, D. J. (1980). Molecular properties of the monoamine oxidases. Schizophrenia Bull. 6, 275-281.
    • (1980) Schizophrenia Bull. , vol.6 , pp. 275-281
    • Edwards, D.J.1
  • 129
    • 0014687522 scopus 로고
    • Interaction of oxidized polyamines with DNA. III. Association with nucleosides, mono- and polynucleotides
    • Eilon, G. and Bachrach, U. (1969). Interaction of oxidized polyamines with DNA. III. Association with nucleosides, mono- and polynucleotides. Biochim. Biophys. Acta 179, 464-472.
    • (1969) Biochim. Biophys. Acta , vol.179 , pp. 464-472
    • Eilon, G.1    Bachrach, U.2
  • 130
    • 0022445963 scopus 로고
    • 1-acetyltransferase in the adrenal cortex of rats following administration of exogenous spermidine, carbamylcholine, 2-deoxyglucose and dopamine agonists
    • 1-acetyltransferase in the adrenal cortex of rats following administration of exogenous spermidine, carbamylcholine, 2-deoxyglucose and dopamine agonists. Biochim. Biophys. Acta 888, 36-41.
    • (1986) Biochim. Biophys. Acta , vol.888 , pp. 36-41
    • Ekker, M.1    Sourkes, T.L.2
  • 131
    • 0024604674 scopus 로고
    • Semicarbazide-sensitive amine oxidase (SSAO) of the rat aorta
    • Elliot, J., Callingham, B. A. and Sharman, D. F. (1989). Semicarbazide-sensitive amine oxidase (SSAO) of the rat aorta. Biochem. Pharmacol. 38, 1507-1515.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 1507-1515
    • Elliot, J.1    Callingham, B.A.2    Sharman, D.F.3
  • 132
    • 0342826389 scopus 로고
    • The detoxicating effect of the liver of cathartes aura upon solutions of β-imidazolylethylamin
    • Eustis, A. C. (1915). The detoxicating effect of the liver of Cathartes aura upon solutions of β-imidazolylethylamin. Biochem. Bull. (N. Y.) 4, 97-99.
    • (1915) Biochem. Bull. (N. Y.) , vol.4 , pp. 97-99
    • Eustis, A.C.1
  • 134
    • 0016616089 scopus 로고
    • Polyamines stabilize DNA folds
    • Flink, I. and Pettijohn, D. E. (1975). Polyamines stabilize DNA folds. Nature 253, 62-63.
    • (1975) Nature , vol.253 , pp. 62-63
    • Flink, I.1    Pettijohn, D.E.2
  • 136
    • 0025654483 scopus 로고
    • Mucosal mono- and polyamine oxidase activities in digestive tract are distributed complementary to diamine oxidase
    • Fogel, W. A. (1990). Mucosal mono- and polyamine oxidase activities in digestive tract are distributed complementary to diamine oxidase. J. Neural Transm. 32 (Suppl.), 345-349.
    • (1990) J. Neural Transm. , vol.32 , Issue.SUPPL. , pp. 345-349
    • Fogel, W.A.1
  • 137
    • 0028985470 scopus 로고
    • Ornithine decarboxylase and S-adenosylmethionine decarboxylase expression during the cell cycle of Chinese hamster ovary cells
    • Fredlund, J. O., Johansson, M. C., Dahlberg, E. and Oredsson, S. M. (1995). Ornithine decarboxylase and S-adenosylmethionine decarboxylase expression during the cell cycle of chinese hamster ovary cells. Exp. Cell. Res. 216, 86-92.
    • (1995) Exp. Cell. Res. , vol.216 , pp. 86-92
    • Fredlund, J.O.1    Johansson, M.C.2    Dahlberg, E.3    Oredsson, S.M.4
  • 138
    • 0021258440 scopus 로고
    • Inhibition of transforming growth factor-induced cell growth in soft agar by oxidised polyamines
    • Frolik, C. A., Roller, P. P., Cone, J. L., Dart, L. L., Smith, D. M. and Sporn, M. B. (1984). Inhibition of transforming growth factor-induced cell growth in soft agar by oxidised polyamines. Arch. Biochem. Biophys. 230, 93-102.
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 93-102
    • Frolik, C.A.1    Roller, P.P.2    Cone, J.L.3    Dart, L.L.4    Smith, D.M.5    Sporn, M.B.6
  • 139
    • 0017069226 scopus 로고
    • The effect of spermidine and spermine on proliferation in vitro of fibroblasts from normal and cyclic fibrosis patients
    • Gahl, W. A., Changus, J. E. and Pitot, H. C. (1976). The effect of spermidine and spermine on proliferation in vitro of fibroblasts from normal and cyclic fibrosis patients. Pediat. Res. 10, 531-535.
    • (1976) Pediat. Res. , vol.10 , pp. 531-535
    • Gahl, W.A.1    Changus, J.E.2    Pitot, H.C.3
  • 140
    • 0018149690 scopus 로고
    • Reversal by aminoguanidine of the inhibition of proliferation of human fibroblasts by spermidine and spermine
    • Gahl, W. A. and Pitot, H. C. (1978). Reversal by aminoguanidine of the inhibition of proliferation of human fibroblasts by spermidine and spermine. Chem.Biol. Interactions 22, 91-98.
    • (1978) Chem.biol. Interactions , vol.22 , pp. 91-98
    • Gahl, W.A.1    Pitot, H.C.2
  • 141
    • 0019812878 scopus 로고
    • Acetylated polyamines as substrates for human pregnancy serum diamine oxidase
    • Gahl, W. A. and Pitot, H. C. (1981). Acetylated polyamines as substrates for human pregnancy serum diamine oxidase. Life Sciences 29, 2177-2179.
    • (1981) Life Sciences , vol.29 , pp. 2177-2179
    • Gahl, W.A.1    Pitot, H.C.2
  • 142
    • 0020079659 scopus 로고
    • Polyamine degradation in foetal and adult bovine serum
    • Gahl, W. A. and Pitot, H. C. (1982). Polyamine degradation in foetal and adult bovine serum. Biochem. J. 202, 603-611.
    • (1982) Biochem. J. , vol.202 , pp. 603-611
    • Gahl, W.A.1    Pitot, H.C.2
  • 143
    • 0019988195 scopus 로고
    • Spermidine oxidase in human pregnancy serum
    • Gahl, W. A., Vale, A. M. and Pitot, H. C. (1982). Spermidine oxidase in human pregnancy serum. Biochem. J. 201, 161-166.
    • (1982) Biochem. J. , vol.201 , pp. 161-166
    • Gahl, W.A.1    Vale, A.M.2    Pitot, H.C.3
  • 144
    • 0022487006 scopus 로고
    • Polyamines and hela-cell DNA replication
    • Gallo, C. J., Koza, R. A. and Herbst, E. J. (1986). Polyamines and HeLa-cell DNA replication. Biochem. J. 238, 37-42.
    • (1986) Biochem. J. , vol.238 , pp. 37-42
    • Gallo, C.J.1    Koza, R.A.2    Herbst, E.J.3
  • 145
    • 0030457242 scopus 로고    scopus 로고
    • Histamine reduces ZO-1 tight-junction protein expression in cultured retinal microvascular endothelial cells
    • Gardner, T. W., Lesher, T., Khin, S., Vu, C., Barber, A. J. and Brennan, W. A. (1996). Histamine reduces ZO-1 tight-junction protein expression in cultured retinal microvascular endothelial cells. Biochem. J. 320, 717-721.
    • (1996) Biochem. J. , vol.320 , pp. 717-721
    • Gardner, T.W.1    Lesher, T.2    Khin, S.3    Vu, C.4    Barber, A.J.5    Brennan, W.A.6
  • 147
    • 0018745592 scopus 로고
    • 1-phase inhibition of cell proliferation
    • 1-phase inhibition of cell proliferation. Br. J. Cancer 39, 548-557.
    • (1978) Br. J. Cancer , vol.39 , pp. 548-557
    • Gaugas, J.M.1    Dewey, D.L.2
  • 148
    • 0018262335 scopus 로고
    • Polyamine interaction with pregnancy serum in suppression of lymphocyte transformation
    • Gaugas, J. M. and Curzen, P. (1978). Polyamine interaction with pregnancy serum in suppression of lymphocyte transformation. Lancet 8054, 18-20.
    • (1978) Lancet , vol.8054 , pp. 18-20
    • Gaugas, J.M.1    Curzen, P.2
  • 149
    • 0003736130 scopus 로고
    • Biogenic diamines and polyamines in support and in inhibition of lymphocyte proliferation
    • (Ed. Gaugas, J. M.), Wiley and Sons, New York
    • Gaugas, J. M. (1980). Biogenic diamines and polyamines in support and in inhibition of lymphocyte proliferation. In "Polyamines in biomedical research" (Ed. Gaugas, J. M.), pp. 343-362, Wiley and Sons, New York.
    • (1980) Polyamines in Biomedical Research , pp. 343-362
    • Gaugas, J.M.1
  • 150
    • 0018973929 scopus 로고
    • Oxygen-dependent free radicals in spermine oxidation cytostasis and chemiluminescence and the role of superoxide dismutase
    • Gaugas, J. M. and Dewey, D. L. (1980). Oxygen-dependent free radicals in spermine oxidation cytostasis and chemiluminescence and the role of superoxide dismutase. Br. J. Cancer 41, 946-955.
    • (1980) Br. J. Cancer , vol.41 , pp. 946-955
    • Gaugas, J.M.1    Dewey, D.L.2
  • 151
    • 0022854553 scopus 로고
    • Polyamines affect growth of cultured rat cerebellar neurons in different sera
    • Gilad, G. M. and Gilad, V. H. (1986). Polyamines affect growth of cultured rat cerebellar neurons in different sera. Int. J. Devl. Neurosci. 4, 195-208.
    • (1986) Int. J. Devl. Neurosci. , vol.4 , pp. 195-208
    • Gilad, G.M.1    Gilad, V.H.2
  • 152
    • 0015864404 scopus 로고
    • Arginase isozymes of rat mammary gland, liver, and other tissues
    • Glass, R. D. and Knox, W. E. (1973). Arginase isozymes of rat mammary gland, liver, and other tissues. J. Biol. Chem. 248, 5785-5789.
    • (1973) J. Biol. Chem. , vol.248 , pp. 5785-5789
    • Glass, R.D.1    Knox, W.E.2
  • 153
    • 0028901121 scopus 로고
    • Detection of quinoproteins after electrophoresis in the presence of urea or SDS
    • Glatz, Z., Janiczek, O., Wimmerová, M. and Novotny, M. V. (1995). Detection of quinoproteins after electrophoresis in the presence of urea or SDS. Biochem. Mol. Biol. Int. 35, 1-10.
    • (1995) Biochem. Mol. Biol. Int. , vol.35 , pp. 1-10
    • Glatz, Z.1    Janiczek, O.2    Wimmerová, M.3    Novotny, M.V.4
  • 154
    • 0014051122 scopus 로고
    • Plasma histaminase activity in various mammalian species; a rapid method of assay
    • Gordon, G. R. and Peters, J. H. (1967). Plasma histaminase activity in various mammalian species; a rapid method of assay. Proc. Soc. Exp. Biol. Med. 124, 399-404.
    • (1967) Proc. Soc. Exp. Biol. Med. , vol.124 , pp. 399-404
    • Gordon, G.R.1    Peters, J.H.2
  • 155
    • 0025285293 scopus 로고
    • Evidence linking programmed cell death in the blastocyst to polyamine oxidation
    • Gramzinski, R. A., Parchment, R. E. and Pierce, G. B. (1990). Evidence linking programmed cell death in the blastocyst to polyamine oxidation. Differentiation 43, 59-65.
    • (1990) Differentiation , vol.43 , pp. 59-65
    • Gramzinski, R.A.1    Parchment, R.E.2    Pierce, G.B.3
  • 157
    • 0017063933 scopus 로고
    • The synthesis and accumulation of polyamines in reproductive prgans of the rat during pregnancy
    • Guha, S. K. and Jänne, J. (1976). The synthesis and accumulation of polyamines in reproductive prgans of the rat during pregnancy. Biochim. Biophys. Acta 437, 244-252.
    • (1976) Biochim. Biophys. Acta , vol.437 , pp. 244-252
    • Guha, S.K.1    Jänne, J.2
  • 158
    • 0014115830 scopus 로고
    • Determination of histaminase activity in histologic samples and its quantitative distribution in intact human placenta and uterus
    • Gunther, R. E. and Glick, D. (1967). Determination of histaminase activity in histologic samples and its quantitative distribution in intact human placenta and uterus. J. Histochem. Cytochem. 15, 431-435.
    • (1967) J. Histochem. Cytochem. , vol.15 , pp. 431-435
    • Gunther, R.E.1    Glick, D.2
  • 159
    • 0030091114 scopus 로고    scopus 로고
    • The isolation and purification of diamine oxidase of pea seedlings and pig liver
    • Güvenilir, Y. A. and Deveci, N. (1996). The isolation and purification of diamine oxidase of pea seedlings and pig liver. Appl. Biochem. Biotechnol. 56, 235-241.
    • (1996) Appl. Biochem. Biotechnol. , vol.56 , pp. 235-241
    • Güvenilir, Y.A.1    Deveci, N.2
  • 160
    • 0023255983 scopus 로고
    • Role of receptors in metabolic interaction of histamine with human vascular endothelial cells and skin fibroblasts
    • Haddock, R. C., Mack, P., Fogerty, F. J. and Baenziger, N. L. (1987). Role of receptors in metabolic interaction of histamine with human vascular endothelial cells and skin fibroblasts. J. Biol. Chem. 262, 10220-10228.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10220-10228
    • Haddock, R.C.1    Mack, P.2    Fogerty, F.J.3    Baenziger, N.L.4
  • 162
    • 0014678162 scopus 로고
    • Plasma diamine oxidase in humans and marmosets
    • Hampton, J. K. and Parmelee, M. L. (1969). Plasma diamine oxidase in humans and marmosets. Comp. Biochem. Physiol. 30, 367-373.
    • (1969) Comp. Biochem. Physiol. , vol.30 , pp. 367-373
    • Hampton, J.K.1    Parmelee, M.L.2
  • 164
    • 0028936790 scopus 로고
    • Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor
    • Hanlon, S. P., Carpenter, K., Hassan, A. and Cooper, R. A. (1995). Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor. Biochem. J. 306, 627-630.
    • (1995) Biochem. J. , vol.306 , pp. 627-630
    • Hanlon, S.P.1    Carpenter, K.2    Hassan, A.3    Cooper, R.A.4
  • 165
    • 0015524977 scopus 로고
    • Polyamine synthesis in the regenerating liver: Stimulation of s-adenosylmethionine decarboxylase, and spermidine and spermine synthases after partial hepatectomy
    • Hannonen, P., Raina, A. and Jänne, J. (1972). Polyamine synthesis in the regenerating liver: Stimulation of S-adenosylmethionine decarboxylase, and spermidine and spermine synthases after partial hepatectomy. Biochim. Biophys. Acta 273, 84-90.
    • (1972) Biochim. Biophys. Acta , vol.273 , pp. 84-90
    • Hannonen, P.1    Raina, A.2    Jänne, J.3
  • 166
    • 0014724952 scopus 로고
    • Diamine oxidase isoenzymes in human blood plasma
    • Hansson, R. (1970). Diamine oxidase isoenzymes in human blood plasma. Scand. J. Clin. Lab. Invest. 25, 33-39.
    • (1970) Scand. J. Clin. Lab. Invest. , vol.25 , pp. 33-39
    • Hansson, R.1
  • 167
    • 0024507640 scopus 로고
    • Heat shock stimulates polyamine oxidation by two distinct mechanisms in mammalian cell cultures
    • Harari, P. M., Fuller, D. J. M., Gerner, E. W. (1989). Heat shock stimulates polyamine oxidation by two distinct mechanisms in mammalian cell cultures. Int. J. Radiat. Oncol. Biol. Phys. 16, 451-457.
    • (1989) Int. J. Radiat. Oncol. Biol. Phys. , vol.16 , pp. 451-457
    • Harari, P.M.1    Fuller, D.J.M.2    Gerner, E.W.3
  • 168
    • 0024321066 scopus 로고
    • Changes in polyamine-oxidising capacity of peroxisomes under various physiological conditions in rats
    • Hayashi, H., Yoshida, H., Hashimoto, F. and Okazeri, S. (1989). Changes in polyamine-oxidising capacity of peroxisomes under various physiological conditions in rats. Biochim. Biophys. Acta 991, 310-316.
    • (1989) Biochim. Biophys. Acta , vol.991 , pp. 310-316
    • Hayashi, H.1    Yoshida, H.2    Hashimoto, F.3    Okazeri, S.4
  • 169
    • 0028910517 scopus 로고
    • Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA
    • He, J. and Furmanski, P. (1995). Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. Nature 373, 721-724.
    • (1995) Nature , vol.373 , pp. 721-724
    • He, J.1    Furmanski, P.2
  • 170
    • 0002302844 scopus 로고
    • Polyamine metabolism in synchronously growing mammalian cells
    • Odense University Press, Odense, Denmark
    • Heby, O., Marton, L. J., Gray, J. W., Lindl, P. A. and Wilson, C. B. (1976). Polyamine metabolism in synchronously growing mammalian cells. Proc. 9. Congr. Nordic Soc. Cell Biol., Odense University Press, pp. 155-164, Odense, Denmark.
    • (1976) Proc. 9. Congr. Nordic Soc. Cell Biol. , pp. 155-164
    • Heby, O.1    Marton, L.J.2    Gray, J.W.3    Lindl, P.A.4    Wilson, C.B.5
  • 171
    • 0343910077 scopus 로고
    • Polyamines and the cell cycle
    • (Ed. Gaugas, J. M.), Wiley and Sons, New York, USA
    • Heby, O. and Andersson, G. (1980). Polyamines and the cell cycle. In "Polyamines in Biomed. Res." (Ed. Gaugas, J. M.), pp. 17-34, Wiley and Sons, New York, USA.
    • (1980) Polyamines in Biomed. Res. , pp. 17-34
    • Heby, O.1    Andersson, G.2
  • 172
    • 0025325255 scopus 로고
    • Molecular genetics of polyamine synthesis in eucaryotic cells
    • Heby, O. and Persson, L. (1990). Molecular genetics of polyamine synthesis in eucaryotic cells. Trends Biochem Sci. 15, 153-158.
    • (1990) Trends Biochem Sci. , vol.15 , pp. 153-158
    • Heby, O.1    Persson, L.2
  • 173
    • 0021714976 scopus 로고
    • Spermidine cytotoxicity in vitro: Effect of serum and oxygen tension
    • Hegre, O. D., Marshall, S. and Hickey, G. E. (1984). Spermidine cytotoxicity in vitro: effect of serum and oxygen tension. In Vitro 20, 198-204.
    • (1984) In Vitro , vol.20 , pp. 198-204
    • Hegre, O.D.1    Marshall, S.2    Hickey, G.E.3
  • 174
    • 0022638678 scopus 로고
    • Mechanism of spermidine cytotoxicity at 37°C and 43°C in chinese hamster ovary cells
    • Henle, K. J., Moss, A. J. and Nagle, W. A. (1986). Mechanism of spermidine cytotoxicity at 37°C and 43°C in Chinese hamster ovary cells. Cancer Res. 46, 175-182.
    • (1986) Cancer Res. , vol.46 , pp. 175-182
    • Henle, K.J.1    Moss, A.J.2    Nagle, W.A.3
  • 175
    • 0019947365 scopus 로고
    • Eosinophil diamine oxidase activity in acute inflammation in humans
    • Herman, J. J. (1982). Eosinophil diamine oxidase activity in acute inflammation in humans. Agents and Actions 12, 46-48.
    • (1982) Agents and Actions , vol.12 , pp. 46-48
    • Herman, J.J.1
  • 176
    • 0021273628 scopus 로고
    • Histamine content, diamine oxidase activity and histamine methyltransferase activity in human tissues: Fact or fiction?
    • Hesterberg, R., Sattler, J., Lorenz, W., Stahlknecht, C.-D., Barth, H., Crombach, M. and Weber, D. (1984). Histamine content, diamine oxidase activity and histamine methyltransferase activity in human tissues: Fact or fiction? Agents and Actions 14, 325-334.
    • (1984) Agents and Actions , vol.14 , pp. 325-334
    • Hesterberg, R.1    Sattler, J.2    Lorenz, W.3    Stahlknecht, C.-D.4    Barth, H.5    Crombach, M.6    Weber, D.7
  • 177
    • 0019366340 scopus 로고
    • Aminoguanidine reversal of the inhibitory effects of ornithine analogs on the in vitro clonogenic survival of the R3327AT prostate-derived tumor
    • Heston, W. D. W., Lazan, D. W. and Fair, W. R. (1981). Aminoguanidine reversal of the inhibitory effects of ornithine analogs on the in vitro clonogenic survival of the R3327AT prostate-derived tumor. Cancer Lett. 11, 323-330.
    • (1981) Cancer Lett. , vol.11 , pp. 323-330
    • Heston, W.D.W.1    Lazan, D.W.2    Fair, W.R.3
  • 178
  • 179
    • 0010692899 scopus 로고
    • Spermine oxidase: An amine oxidase with specificity for spermine and spermidine
    • Hirsch, J. G. (1953). Spermine oxidase: An amine oxidase with specificity for spermine and spermidine. J. Exp. Med. 97, 345-355.
    • (1953) J. Exp. Med. , vol.97 , pp. 345-355
    • Hirsch, J.G.1
  • 180
    • 0024546803 scopus 로고
    • Characterization of difluoromethylor-nithine-resistant mouse and human tumor cell lines
    • Hirvonen, A., Eloranta, T., Hyvönen, T., Alhonen, L. and Jänne, J. (1989). Characterization of difluoromethylor-nithine-resistant mouse and human tumor cell lines. Biochem. J. 258, 709-713.
    • (1989) Biochem. J. , vol.258 , pp. 709-713
    • Hirvonen, A.1    Eloranta, T.2    Hyvönen, T.3    Alhonen, L.J.J.4
  • 181
    • 0021748570 scopus 로고
    • Histamine uptake and metabolism in the blood vessels of rats
    • Holcslaw, T., Wilson, C. and Nichols, G. (1984). Histamine uptake and metabolism in the blood vessels of rats. Agents and Actions 15, 202-210.
    • (1984) Agents and Actions , vol.15 , pp. 202-210
    • Holcslaw, T.1    Wilson, C.2    Nichols, G.3
  • 182
    • 0021222518 scopus 로고
    • Diamine oxidase activity in human decidua and endometrium
    • Holinka, C. F. and Gurpide, E. (1984). Diamine oxidase activity in human decidua and endometrium. Am. J. Obstet. Gynecol. 150, 359-363.
    • (1984) Am. J. Obstet. Gynecol. , vol.150 , pp. 359-363
    • Holinka, C.F.1    Gurpide, E.2
  • 183
    • 0028182813 scopus 로고
    • Location of the active site of rat vascular semicarbazide-sensitive amine oxidase
    • Holt, A. and Callingham, B. A. (1994). Location of the active site of rat vascular semicarbazide-sensitive amine oxidase. J. Neural. Transm. 41, 433-437.
    • (1994) J. Neural. Transm. , vol.41 , pp. 433-437
    • Holt, A.1    Callingham, B.A.2
  • 184
    • 0032492682 scopus 로고    scopus 로고
    • Identification of the quinone cofactor in mammalian semicarbazide-sensitive amine oxidase
    • Holt, A., Alton, G., Seaman, C. H., Loppnow, G. R., Szpacenko, A., Svendsen, I. and Palcic, M. M. (1998). Identification of the quinone cofactor in mammalian semicarbazide-sensitive amine oxidase. Biochemistry 37, 4946-4957.
    • (1998) Biochemistry , vol.37 , pp. 4946-4957
    • Holt, A.1    Alton, G.2    Seaman, C.H.3    Loppnow, G.R.4    Szpacenko, A.5    Svendsen, I.6    Palcic, M.M.7
  • 185
    • 38249026003 scopus 로고
    • Oxidation of polyamines by pyrroloquinoline quinone (PQQ)
    • Houen, G., Larsen, C. and Larsson, L.-I. (1989). Oxidation of polyamines by pyrroloquinoline quinone (PQQ). Tetrahedron 45, 4235-4242.
    • (1989) Tetrahedron , vol.45 , pp. 4235-4242
    • Houen, G.1    Larsen, C.2    Larsson, L.-I.3
  • 186
    • 0026622865 scopus 로고
    • A specific peroxidase coupled activity stain for amine oxidases
    • Houen, G. and Leonardsen, L. (1992). A specific peroxidase coupled activity stain for amine oxidases. Anal. Biochem. 204, 296-299.
    • (1992) Anal. Biochem. , vol.204 , pp. 296-299
    • Houen, G.1    Leonardsen, L.2
  • 187
    • 0027670396 scopus 로고
    • Purification and partial characterization of mammalian Cu-dependent amine oxidases
    • Houen, G., Jørgensen, J., Leonardsen, L. and Larsson, L.-I. (1993). Purification and partial characterization of mammalian Cu-dependent amine oxidases. Acta Chem. Scand. 47, 902-909.
    • (1993) Acta Chem. Scand. , vol.47 , pp. 902-909
    • Houen, G.1    Jørgensen, J.2    Leonardsen, L.3    Larsson, L.-I.4
  • 188
    • 0028137994 scopus 로고
    • HPLC and NMR investigation of the serum amine oxidase catalyzed oxidation of polyamines
    • Houen, G., Bock, K. and Jensen, A. L. (1994). HPLC and NMR investigation of the serum amine oxidase catalyzed oxidation of polyamines. Acta Chem. Scand. 48, 52-60.
    • (1994) Acta Chem. Scand. , vol.48 , pp. 52-60
    • Houen, G.1    Bock, K.2    Jensen, A.L.3
  • 189
    • 0029825422 scopus 로고    scopus 로고
    • Lactoferrin: Similarity to diamine oxidase and purification by aminohexyl affinity chromatography
    • Houen, G., Høgdall, E. V. S., Barkholt, V. and Nørskov, L. (1996). Lactoferrin: Similarity to diamine oxidase and purification by aminohexyl affinity chromatography. Eur. J. Biochem. 241, 303-308.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 303-308
    • Houen, G.1    Høgdall, E.V.S.2    Barkholt, V.3    Nørskov, L.4
  • 190
    • 0027096560 scopus 로고
    • Polyamine cytochemistry: Localization and possible functions of polyamines
    • Hougaard, D. M. (1992). Polyamine cytochemistry: localization and possible functions of polyamines. Int. Rev. Cytol. 138, 51-88.
    • (1992) Int. Rev. Cytol. , vol.138 , pp. 51-88
    • Hougaard, D.M.1
  • 191
    • 0026695053 scopus 로고
    • Regulation of gastric mucosal diamine oxidase activity by gastrin
    • Hougaard, D. M., Houen, G. and Larsson, L.-I. (1992). Regulation of gastric mucosal diamine oxidase activity by gastrin. FEBS Lett. 307, 135-138.
    • (1992) FEBS Lett. , vol.307 , pp. 135-138
    • Hougaard, D.M.1    Houen, G.2    Larsson, L.-I.3
  • 192
    • 0021065561 scopus 로고
    • Polyamine-mediated inhibition of in-vitro cell proliferation is not due to acrolein
    • Hussain, J. I., Smith, C. J. and Allen, J. C. (1983). Polyamine-mediated inhibition of in-vitro cell proliferation is not due to acrolein. Cell Tissue Kinet. 16, 583-591.
    • (1983) Cell Tissue Kinet. , vol.16 , pp. 583-591
    • Hussain, J.I.1    Smith, C.J.2    Allen, J.C.3
  • 193
    • 0024792327 scopus 로고
    • Rapid purification of porcine colostral whey lactoferrin by affinity chromatography on single-stranded DNA-agarose. Characterization, amino acid composition and N-terminal sequence
    • Hutchens, T. W., Magnuson, J. S. and Yip, T.-T. (1989a). Rapid purification of porcine colostral whey lactoferrin by affinity chromatography on single-stranded DNA-agarose. Characterization, amino acid composition and N-terminal sequence. Biochim. Biophys. Acta 999, 323-329.
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 323-329
    • Hutchens, T.W.1    Magnuson, J.S.2    Yip, T.-T.3
  • 194
    • 0024398309 scopus 로고
    • Interaction of human lactoferrin with DNA: One-step purification by affinity chromatography on single-stranded DNA-agarose
    • Hutchens, T. W., Magnuson, J. S. and Yip, T.-T. (1989b). Interaction of human lactoferrin with DNA: One-step purification by affinity chromatography on single-stranded DNA-agarose. Pediat. Res. 26, 618-622.
    • (1989) Pediat. Res. , vol.26 , pp. 618-622
    • Hutchens, T.W.1    Magnuson, J.S.2    Yip, T.-T.3
  • 195
    • 0023245114 scopus 로고
    • In vitro expression of benzylamine oxidase activity in cultured porcine smooth muscle cells
    • Hysmith, R. M. and Boor, P. J. (1987). In vitro expression of benzylamine oxidase activity in cultured porcine smooth muscle cells. J. Cardiovasc. Pharmacol. 9, 668-674.
    • (1987) J. Cardiovasc. Pharmacol. , vol.9 , pp. 668-674
    • Hysmith, R.M.1    Boor, P.J.2
  • 196
    • 0032518328 scopus 로고    scopus 로고
    • Structure and tissue-specific expression of genes encoding bovine copper amine oxidases
    • Høgdall, E. V. S., Houen, G., Borre, M., Bundgaard, J. R., Larsson, L.-I. and Vuust, J. (1998). Structure and tissue-specific expression of genes encoding bovine copper amine oxidases. Eur. J. Biochem. 251, 320-328.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 320-328
    • Høgdall, E.V.S.1    Houen, G.2    Borre, M.3    Bundgaard, J.R.4    Larsson, L.-I.5    Vuust, J.6
  • 197
    • 0016593558 scopus 로고
    • Oxidation of polyamines by diamine oxidase from human seminal plasma
    • Hölttä, E., Pulkkinen, P., Elfving, K. and Jänne, J. (1975). Oxidation of polyamines by diamine oxidase from human seminal plasma. Biochem. J. 145, 373-378.
    • (1975) Biochem. J. , vol.145 , pp. 373-378
    • Hölttä, E.1    Pulkkinen, P.2    Elfving, K.3    Jänne, J.4
  • 198
    • 0017623867 scopus 로고
    • Oxidation of spermidine and spermine in rat liver: Purification and properties of polyamine oxidase
    • Hölttä, E. (1977). Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase. Biochemistry 16, 91-100.
    • (1977) Biochemistry , vol.16 , pp. 91-100
    • Hölttä, E.1
  • 199
    • 0020455519 scopus 로고
    • Polyamine dependence of chinese hamster ovary cells in serum-free culture is due to deficient arginase activity
    • Hölttä, E. and Pohjanpelto, P. (1982). Polyamine dependence of chinese hamster ovary cells in serum-free culture is due to deficient arginase activity. Biochim. Biophys. Acta 721, 321-327.
    • (1982) Biochim. Biophys. Acta , vol.721 , pp. 321-327
    • Hölttä, E.1    Pohjanpelto, P.2
  • 200
    • 0020643526 scopus 로고
    • Polyamine oxidase (rat liver)
    • Hölttä, E. (1983). Polyamine oxidase (rat liver). Meth. Enzymol. 94, 306-311.
    • (1983) Meth. Enzymol. , vol.94 , pp. 306-311
    • Hölttä, E.1
  • 201
    • 0023720253 scopus 로고
    • Induction and quail liver diamine oxidase (histaminase). Part I: Interference of spermidine synthase on the diamine oxidase activity using putrescine as substrate
    • Ignesti, G., Perretti, M. and Buffoni, F. (1988). Induction and quail liver diamine oxidase (histaminase). Part I: interference of spermidine synthase on the diamine oxidase activity using putrescine as substrate. Agents and Actions 25, 37-47.
    • (1988) Agents and Actions , vol.25 , pp. 37-47
    • Ignesti, G.1    Perretti, M.2    Buffoni, F.3
  • 202
    • 0027380981 scopus 로고
    • Some problems with the diamine oxidase (DAO) assay using putrescine as substrate in rat liver
    • Ignesti, G., Banchelli, G., Pirisino, R., Raimondi, L. and Buffoni, F. (1993). Some problems with the diamine oxidase (DAO) assay using putrescine as substrate in rat liver. Agents and Actions 39, 7-12.
    • (1993) Agents and Actions , vol.39 , pp. 7-12
    • Ignesti, G.1    Banchelli, G.2    Pirisino, R.3    Raimondi, L.4    Buffoni, F.5
  • 203
    • 0018728492 scopus 로고
    • Polyamine oxidase activity in human pregnancy serum
    • Illei, G. and Morgan, D. M. L. (1979). Polyamine oxidase activity in human pregnancy serum. Br. J. Obstet. Gynaecol. 86, 878-881.
    • (1979) Br. J. Obstet. Gynaecol. , vol.86 , pp. 878-881
    • Illei, G.1    Morgan, D.M.L.2
  • 204
    • 0031106170 scopus 로고    scopus 로고
    • Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping
    • Imamura, Y., Kubota, R., Wang, Y., Asakawa, S., Kudoh, J., Mashima, Y., Oguchi, Y. and Shimizu, N. (1997). Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping. Genomics 40, 277-283.
    • (1997) Genomics , vol.40 , pp. 277-283
    • Imamura, Y.1    Kubota, R.2    Wang, Y.3    Asakawa, S.4    Kudoh, J.5    Mashima, Y.6    Oguchi, Y.7    Shimizu, N.8
  • 205
    • 0032528287 scopus 로고    scopus 로고
    • Human retina-specific amine oxidase: Genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina
    • Imamura, Y., Noda, S., Mashima, Y., Kudoh, J., Oguchi, Y. and Shimizu, N. (1998). Human retina-specific amine oxidase: Genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina. Genomics 51, 293-298.
    • (1998) Genomics , vol.51 , pp. 293-298
    • Imamura, Y.1    Noda, S.2    Mashima, Y.3    Kudoh, J.4    Oguchi, Y.5    Shimizu, N.6
  • 206
    • 0019322002 scopus 로고
    • Bovine plasma amine oxidase interactions with concanavalin A in solution and with concanavalin A-sepharose
    • Ishizaki, H. and Yyasunobu, K. T. (1980). Bovine plasma amine oxidase interactions with concanavalin A in solution and with concanavalin A-Sepharose. Biochim. Biophys. Acta 611, 27-34.
    • (1980) Biochim. Biophys. Acta , vol.611 , pp. 27-34
    • Ishizaki, H.1    Yyasunobu, K.T.2
  • 207
    • 0015150607 scopus 로고
    • Synthesis of aminoethyl derivatives of α,ω-alkylenediamines and structure-activity relationships for the polyamine-bovine plasma amine oxidase system
    • Israel, M. and Modest, E. J. (1971). Synthesis of aminoethyl derivatives of α,ω-alkylenediamines and structure-activity relationships for the polyamine-bovine plasma amine oxidase system. J.Med. Chem. 14, 1042-1047.
    • (1971) J.med. Chem. , vol.14 , pp. 1042-1047
    • Israel, M.1    Modest, E.J.2
  • 209
    • 0025346921 scopus 로고
    • Polyamine regulation of the synthesis of thymidine kinase in bovine lymphocytes
    • Ito, K. and Igarashi, K. (1990). Polyamine regulation of the synthesis of thymidine kinase in bovine lymphocytes. Arch. Biochem. Biophys. 278, 277-283.
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 277-283
    • Ito, K.1    Igarashi, K.2
  • 210
    • 0025374783 scopus 로고
    • A new redox cofactor in eucaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase
    • Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur, S., Maltby, D., Burlingame, A. L. and Klinman, J. P. (1990). A new redox cofactor in eucaryotic enzymes: 6-Hydroxydopa at the active site of bovine serum amine oxidase. Science 248, 981-987.
    • (1990) Science , vol.248 , pp. 981-987
    • Janes, S.M.1    Mu, D.2    Wemmer, D.3    Smith, A.J.4    Kaur, S.5    Maltby, D.6    Burlingame, A.L.7    Klinman, J.P.8
  • 213
    • 0029332131 scopus 로고
    • The major integral membrane glycoprotein in adipocytes is a novel 200-kDa heterodimer
    • Jochen, A., Guven, S. and Hays, J. (1995). The major integral membrane glycoprotein in adipocytes is a novel 200-kDa heterodimer. Mol. Membrane Biol. 12, 277-281.
    • (1995) Mol. Membrane Biol. , vol.12 , pp. 277-281
    • Jochen, A.1    Guven, S.2    Hays, J.3
  • 215
    • 0029438563 scopus 로고
    • Catalytic properties and structural components of lysyl oxidase
    • The molecular biology and pathology of elastic tissues Wiley and Sons, New York, USA
    • Kagan, H. M., Reddy, V. B., Narasimhan, N. and Csiszar, K. (1995). Catalytic properties and structural components of lysyl oxidase. In "The molecular biology and pathology of elastic tissues", Ciba Found. Symp. 192, pp. 100-121, Wiley and Sons, New York, USA.
    • (1995) Ciba Found. Symp. , vol.192 , pp. 100-121
    • Kagan, H.M.1    Reddy, V.B.2    Narasimhan, N.3    Csiszar, K.4
  • 216
    • 0002312131 scopus 로고
    • Increased formation of histamine in the pregnant rat
    • Kahlson, G., Rosengren, E. and Westling, H. (1958). Increased formation of histamine in the pregnant rat. J. Physiol. 143, 91-103.
    • (1958) J. Physiol. , vol.143 , pp. 91-103
    • Kahlson, G.1    Rosengren, E.2    Westling, H.3
  • 217
    • 0023049897 scopus 로고
    • Effects of polyamines on in vitro reconstitution of ribosomal subunits
    • Kakegawa, T., Hirose, S., Kashiwagi, K. and Igarashi, K. (1986). Effects of polyamines on in vitro reconstitution of ribosomal subunits. Eur. J. Biochem. 158, 265-269.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 265-269
    • Kakegawa, T.1    Hirose, S.2    Kashiwagi, K.3    Igarashi, K.4
  • 218
    • 0023664053 scopus 로고
    • Inhibition of translation of mRNAs for ornithine decarboxylase and S-adenosyl-methionine decarboxylase by polyamines
    • Kameji, T. and Pegg, A. E. (1987). Inhibition of translation of mRNAs for ornithine decarboxylase and S-adenosyl-methionine decarboxylase by polyamines. J. Biol. Chem. 262, 2427-2430.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2427-2430
    • Kameji, T.1    Pegg, A.E.2
  • 219
    • 0027190435 scopus 로고
    • Spermidine-induced destabilization of ornithine decarboxylase (ODC) is mediated by accumulation of antizyme in ODC-overproducing variant cells
    • Kanamoto, R., Kameji, T., Iwashita, S., Igarashi, K. and Hayashi, S. (1993). Spermidine-induced destabilization of ornithine decarboxylase (ODC) is mediated by accumulation of antizyme in ODC-overproducing variant cells. J. Biol. Chem. 268, 9393-9399.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9393-9399
    • Kanamoto, R.1    Kameji, T.2    Iwashita, S.3    Igarashi, K.4    Hayashi, S.5
  • 220
    • 0342826380 scopus 로고
    • Purification and identification of hog kidney histaminase
    • Kapeller-Adler, R. and Macfarlane, H. (1963). Purification and identification of hog kidney histaminase. Biochem. Biophys. Acta 67, 542-565.
    • (1963) Biochem. Biophys. Acta , vol.67 , pp. 542-565
    • Kapeller-Adler, R.1    Macfarlane, H.2
  • 224
    • 0014592508 scopus 로고
    • Distribution of diamine oxidase and imidazole-N-methyltransferase along the gastrointestinal tract
    • Kim, K. S., Backus, B., Harris, M. and Rourke, P. (1969). Distribution of diamine oxidase and imidazole-N-methyltransferase along the gastrointestinal tract. Comp. Biochem. Physiol. 31, 137-145.
    • (1969) Comp. Biochem. Physiol. , vol.31 , pp. 137-145
    • Kim, K.S.1    Backus, B.2    Harris, M.3    Rourke, P.4
  • 225
    • 0014984818 scopus 로고
    • Preparation and stability of oxidized polyamines
    • Kimes, B. W. and Morris, D. R. (1971a). Preparation and stability of oxidized polyamines. Biochim. Biophys. Acta 228, 223-234.
    • (1971) Biochim. Biophys. Acta , vol.228 , pp. 223-234
    • Kimes, B.W.1    Morris, D.R.2
  • 226
    • 0014981738 scopus 로고
    • Inhibition of nucleic acid and protein synthesis in Escherichia coli by oxidised polyamines and acrolein
    • Kimes, B. W. and Morris, D. R. (1971b). Inhibition of nucleic acid and protein synthesis in Escherichia coli by oxidised polyamines and acrolein. Biochim. Biophys. Acta 228, 235-244.
    • (1971) Biochim. Biophys. Acta , vol.228 , pp. 235-244
    • Kimes, B.W.1    Morris, D.R.2
  • 227
    • 0028244179 scopus 로고
    • Quinoenzymes in biology
    • Klinman, J. P. and Mu, D. (1994). Quinoenzymes in biology. Annu. Rev. Biochem. 63, 299-344.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 299-344
    • Klinman, J.P.1    Mu, D.2
  • 228
    • 0029911030 scopus 로고    scopus 로고
    • New quinocofactors in eucaryotes
    • Klinman, J. P. (1996). New quinocofactors in eucaryotes. J. Biol. Chem. 271, 27189-27192.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27189-27192
    • Klinman, J.P.1
  • 229
    • 0017402281 scopus 로고
    • Diamine oxidase: Molecular weight and subunit analysis
    • Kluetz, M. D. and Schmidt, P. G. (1977). Diamine oxidase: Molecular weight and subunit analysis. Biochem. Biophys. Res. Commun. 76, 40-45.
    • (1977) Biochem. Biophys. Res. Commun. , vol.76 , pp. 40-45
    • Kluetz, M.D.1    Schmidt, P.G.2
  • 230
    • 0001166155 scopus 로고
    • Amine oxidases
    • (Eds. Sigel, H. and Sigel, A.), Marcel Dekker, New York, USA
    • Knowles, P. F. and Dooley, D. M. (1994). Amine oxidases. In "Metal ions in biological systems" Vol. 30 (Eds. Sigel, H. and Sigel, A.), pp. 361-403, Marcel Dekker, New York, USA.
    • (1994) Metal Ions in Biological Systems , vol.30 , pp. 361-403
    • Knowles, P.F.1    Dooley, D.M.2
  • 231
    • 0342391646 scopus 로고
    • Plasma diamine oxidase titres of normal and pregnant rats
    • Kobayashi, Y. (1964). Plasma diamine oxidase titres of normal and pregnant rats. Nature 203, 146-147.
    • (1964) Nature , vol.203 , pp. 146-147
    • Kobayashi, Y.1
  • 232
    • 0029020034 scopus 로고
    • Purification of human hepatic arginase and its manganese (II)-dependent interconversion between active and inactive forms: A possible pH-sensing function of the enzyme on the ornithine cycle
    • Kuhn, N. J., Ward, S., Piponski, M. and Young, T. W. (1995). Purification of human hepatic arginase and its manganese (II)-dependent interconversion between active and inactive forms: a possible pH-sensing function of the enzyme on the ornithine cycle. Arch. Biochem. Biophys. 320, 24-34.
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 24-34
    • Kuhn, N.J.1    Ward, S.2    Piponski, M.3    Young, T.W.4
  • 233
    • 0025290570 scopus 로고
    • A radioisotopic assay for polyamine oxidase
    • Kumazawa, T., Seno, H. and Suzuki, O. (1990). A radioisotopic assay for polyamine oxidase. Anal. Biochem. 188, 105-108.
    • (1990) Anal. Biochem. , vol.188 , pp. 105-108
    • Kumazawa, T.1    Seno, H.2    Suzuki, O.3
  • 234
    • 0032146777 scopus 로고    scopus 로고
    • Circulating form of human vascular adhesion protein-1 (VAP-1): Increased serum levels in inflammatory liver diseases
    • Kurkijarvi, R., Adams, D. H., Leino, R., Mottonen, T., Jalkanen, S. and Salmi, M. (1998). Circulating form of human vascular adhesion protein-1 (VAP-1): Increased serum levels in inflammatory liver diseases. J. Immunol. 161, 1549-1557.
    • (1998) J. Immunol. , vol.161 , pp. 1549-1557
    • Kurkijarvi, R.1    Adams, D.H.2    Leino, R.3    Mottonen, T.4    Jalkanen, S.5    Salmi, M.6
  • 235
    • 0015698818 scopus 로고
    • 14C-putrescine assay with the NADH test for the determination of diamine oxidase: Description of a standard procedure with high precision and an improved accuracy
    • 14C-putrescine assay with the NADH test for the determination of diamine oxidase: description of a standard procedure with high precision and an improved accuracy. Agents and Actions 3, 148-156.
    • (1973) Agents and Actions , vol.3 , pp. 148-156
    • Kusche, J.1    Richter, H.2    Hesterberg, R.3    Schmidt, J.4    Lorenz, W.5
  • 236
    • 0016783743 scopus 로고
    • Diamine oxidases in the small intestine of rabbits, dogs and pigs: Separation from soluble monoamine oxidases and substrate specificity of the enzymes
    • Kusche, J., Schmidt, J., Schmidt, A. and Lorenz, W. (1975a). Diamine oxidases in the small intestine of rabbits, dogs and pigs: Separation from soluble monoamine oxidases and substrate specificity of the enzymes. Agents and Actions 5, 440-441.
    • (1975) Agents and Actions , vol.5 , pp. 440-441
    • Kusche, J.1    Schmidt, J.2    Schmidt, A.3    Lorenz, W.4
  • 237
    • 0016590045 scopus 로고
    • Diamine oxidase in rabbit small intestine: Separation from a soluble monoamine oxidase, properties and pathophysiological significance in intestinal ischemia
    • Kushe, J., Richter, H., Schmidt, J., Hesterberg, R., Friedrich, A. and Lorenz, W. (1975b). Diamine oxidase in rabbit small intestine: Separation from a soluble monoamine oxidase, properties and pathophysiological significance in intestinal ischemia. Agents and Actions 5, 431-439.
    • (1975) Agents and Actions , vol.5 , pp. 431-439
    • Kushe, J.1    Richter, H.2    Schmidt, J.3    Hesterberg, R.4    Friedrich, A.5    Lorenz, W.6
  • 238
    • 0019505949 scopus 로고
    • Enzymatic oxidation of polyamines. Relationship to immunosuppressive properties
    • Labib, R. S. and Tomasi, T. B. (1981). Enzymatic oxidation of polyamines. Relationship to immunosuppressive properties. Eur. J. Immunol. 11, 266-269.
    • (1981) Eur. J. Immunol. , vol.11 , pp. 266-269
    • Labib, R.S.1    Tomasi, T.B.2
  • 239
    • 0342826376 scopus 로고
    • Oxygen consumption during the histamine-histaminase reaction
    • Laskowski, M. (1942). Oxygen consumption during the histamine-histaminase reaction. J. Biol. Chem. 145, 457-461.
    • (1942) J. Biol. Chem. , vol.145 , pp. 457-461
    • Laskowski, M.1
  • 240
    • 0025115344 scopus 로고
    • Purification, characterisation, and structural elucidation of the active moiety of the previously called "suppressor activating factor (SAF)"
    • Lau, C., Stanojev, D., Visconti, V., Pang, H., Krepinsky, G., Grey, A., Wang, E. and Ishaque, A. (1990). Purification, characterisation, and structural elucidation of the active moiety of the previously called "suppressor activating factor (SAF)". Cell. Immunol. 125, 92-106.
    • (1990) Cell. Immunol. , vol.125 , pp. 92-106
    • Lau, C.1    Stanojev, D.2    Visconti, V.3    Pang, H.4    Krepinsky, G.5    Grey, A.6    Wang, E.7    Ishaque, A.8
  • 241
    • 0032584718 scopus 로고    scopus 로고
    • Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini
    • Lee, Y. and Sayre, L. M. (1998). Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini. J. Biol. Chem. 273, 19490-19494.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19490-19494
    • Lee, Y.1    Sayre, L.M.2
  • 242
    • 0023122976 scopus 로고
    • Human myeloma cells acquire resistance to difluoromethylornithine by amplification of omithine decarboxylase gene
    • Leinonen, P., Alhonen-Hongistu, L., Laine, R., Jänne, O. A. and Jänne, J. (1987). Human myeloma cells acquire resistance to difluoromethylornithine by amplification of omithine decarboxylase gene. Biochem. J. 242, 199-203.
    • (1987) Biochem. J. , vol.242 , pp. 199-203
    • Leinonen, P.1    Alhonen-Hongistu, L.2    Laine, R.3    Jänne, O.A.4    Jänne, J.5
  • 243
    • 0023183179 scopus 로고
    • Separation of two isozymes of polyamine oxidase from murine L1210 leukemia cells
    • Libby, P. R. and Porter, C. W. (1987). Separation of two isozymes of polyamine oxidase from murine L1210 leukemia cells. Biochem. Biophys. Res. Coomun. 144, 528-585.
    • (1987) Biochem. Biophys. Res. Coomun. , vol.144 , pp. 528-585
    • Libby, P.R.1    Porter, C.W.2
  • 244
    • 0016605260 scopus 로고
    • A simple method to identify plasma amine oxidase activity band on polyacrylamide gel
    • Lin, A. W. M. and Castell, D, O. (1975). A simple method to identify plasma amine oxidase activity band on polyacrylamide gel. Anal. Biochem. 69, 637-642.
    • (1975) Anal. Biochem. , vol.69 , pp. 637-642
    • Lin, A.W.M.1    Castell, D.2
  • 245
    • 0018238723 scopus 로고
    • Immunofluorescent staining of histaminase (diamine oxidase) in human placenta
    • Lin, C.-W., Chapman, C. M., DeLellis, R. A. and Kirley, S. (1978). Immunofluorescent staining of histaminase (diamine oxidase) in human placenta. J. Histochem. Cytochem. 26, 1021-1025.
    • (1978) J. Histochem. Cytochem. , vol.26 , pp. 1021-1025
    • Lin, C.-W.1    Chapman, C.M.2    Delellis, R.A.3    Kirley, S.4
  • 246
    • 0019858565 scopus 로고
    • Tumor and placental histaminase. I. Affinity chromatography purification and characterisation of the placental enzyme
    • Lin, C.-W., Kirley, S. D. and St. Pierre, M. (1981). Tumor and placental histaminase. I. Affinity chromatography purification and characterisation of the placental enzyme. Oncodevelopm. Biol. Med. 2, 267-280.
    • (1981) Oncodevelopm. Biol. Med. , vol.2 , pp. 267-280
    • Lin, C.-W.1    Kirley, S.D.2    St. Pierre, M.3
  • 247
    • 0026655335 scopus 로고
    • Aldehyde dehydrogenases and their role in carcinogenesis
    • Lindahl, R. (1992). Aldehyde dehydrogenases and their role in carcinogenesis. Crit. Rev. Biochem. Mol. Biol. 27, 283-335.
    • (1992) Crit. Rev. Biochem. Mol. Biol. , vol.27 , pp. 283-335
    • Lindahl, R.1
  • 248
    • 0027218504 scopus 로고
    • Molecular cloning and functional expression of different molecular forms of rat amilorid-binding proteins
    • Lingueglia, E., Renard, S., Voilley, N., Waldmann, R., Chassande, O., Lazdunski, M. and Barbry, P. (1993). Molecular cloning and functional expression of different molecular forms of rat amilorid-binding proteins. Eur. J. Biochem. 216, 679-687.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 679-687
    • Lingueglia, E.1    Renard, S.2    Voilley, N.3    Waldmann, R.4    Chassande, O.5    Lazdunski, M.6    Barbry, P.7
  • 249
    • 0027160213 scopus 로고
    • Inhibition of programmed cell death by catalase and phenylalanine methyl ester
    • Little, G. H. and Floris, A. (1993). Inhibition of programmed cell death by catalase and phenylalanine methyl ester. Comp. Biochem. Physiol. 105A, 79-83.
    • (1993) Comp. Biochem. Physiol. , vol.105 A , pp. 79-83
    • Little, G.H.1    Floris, A.2
  • 251
    • 0025959813 scopus 로고
    • The oxidation of dopamine by the semicarbazide-sensitive amine oxidase (SSAO) from rat vas deferens
    • Lizcano, J. M., Balsa, D., Tipton, K. F. and Unzeta, M. (1991). The oxidation of dopamine by the semicarbazide-sensitive amine oxidase (SSAO) from rat vas deferens. Biochem. Pharmacol. 41, 1107-1110.
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 1107-1110
    • Lizcano, J.M.1    Balsa, D.2    Tipton, K.F.3    Unzeta, M.4
  • 252
    • 0028249243 scopus 로고
    • Several aspects on the amine oxidation by semicarbazide-sensitive amine oxidase (SSAO) from bovine lung
    • Lizcano, J. M., de Arriba, A. F., Lyles, G. A. and Unzeta, M. (1994). Several aspects on the amine oxidation by semicarbazide-sensitive amine oxidase (SSAO) from bovine lung. J. Neural. Transm. 41, 415-420.
    • (1994) J. Neural. Transm. , vol.41 , pp. 415-420
    • Lizcano, J.M.1    De Arriba, A.F.2    Lyles, G.A.3    Unzeta, M.4
  • 253
    • 0030602859 scopus 로고    scopus 로고
    • Inhibition of bovine lung semicarbazide-sensitive amine oxidase (SSAO) by some hydrazine derivatives
    • Lizcano, J. M., de Arriba, A. F., Tipton, K. F. and Unzeta, M. (1996). Inhibition of bovine lung semicarbazide-sensitive amine oxidase (SSAO) by some hydrazine derivatives. Biochem. Pharmacol. 52, 187-195.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 187-195
    • Lizcano, J.M.1    De Arriba, A.F.2    Tipton, K.F.3    Unzeta, M.4
  • 254
    • 0032055852 scopus 로고    scopus 로고
    • Purification and characterisation of membrane-bound semi-carbazide-sensitive amine oxidase (SSAO) from bovine lung
    • Lizcano, J. M., Tipton, K. F. and Unzeta, M. (1998). Purification and characterisation of membrane-bound semi-carbazide-sensitive amine oxidase (SSAO) from bovine lung. Biochem. J. 331, 69-78.
    • (1998) Biochem. J. , vol.331 , pp. 69-78
    • Lizcano, J.M.1    Tipton, K.F.2    Unzeta, M.3
  • 255
    • 0023213621 scopus 로고
    • Extended culture of mouse embryo cells without serum: Inhibition by serum
    • Loo, D. T., Fuquat, J. I., Rawson, C. L. and Barnes, D. W. (1987). Extended culture of mouse embryo cells without serum: Inhibition by serum. Science 236, 200-202.
    • (1987) Science , vol.236 , pp. 200-202
    • Loo, D.T.1    Fuquat, J.I.2    Rawson, C.L.3    Barnes, D.W.4
  • 256
    • 0014652183 scopus 로고
    • Biochemical and histochemical studies on the distribution of histamine in the digestive tract of man, dog and other mammals
    • Lorenz, W., Schauer, A., Heitland, S., Calvoer, R. and Werle, E. (1969). Biochemical and histochemical studies on the distribution of histamine in the digestive tract of man, dog and other mammals. Naunyn-Schmiedebergs Arch. Pharmakol. 265, 81-100.
    • (1969) Naunyn-Schmiedebergs Arch. Pharmakol. , vol.265 , pp. 81-100
    • Lorenz, W.1    Schauer, A.2    Heitland, S.3    Calvoer, R.4    Werle, E.5
  • 257
    • 0023464092 scopus 로고
    • Polyamines in intestinal and pancreatic adaption
    • Luk, G. D. and Yang, P. (1987). Polyamines in intestinal and pancreatic adaption. Gut 28, 95-101.
    • (1987) Gut , vol.28 , pp. 95-101
    • Luk, G.D.1    Yang, P.2
  • 258
    • 0020682166 scopus 로고
    • Polyamines in early embryonic development: Their relationship to nuclear multiplication rate, cell cycle traverse, and nucleolar formation in a dipteran egg
    • Lundquist, A., Löwkvist, B., Linden, M. and Heby, O. (1983). Polyamines in early embryonic development: their relationship to nuclear multiplication rate, cell cycle traverse, and nucleolar formation in a dipteran egg. Developm. Biol. 95, 253-259.
    • (1983) Developm. Biol. , vol.95 , pp. 253-259
    • Lundquist, A.1    Löwkvist, B.2    Linden, M.3    Heby, O.4
  • 259
    • 0021963287 scopus 로고
    • An allylamine derivative (MDL 72145) with potent irreversible inhibitory actions on rat aorta semicarbazide-sensitive amine oxidase
    • Lyles, G. A. and Fitcpatrick, C. M. S. (1985). An allylamine derivative (MDL 72145) with potent irreversible inhibitory actions on rat aorta semicarbazide-sensitive amine oxidase. J. Pharm. Pharmacol. 37, 329-335.
    • (1985) J. Pharm. Pharmacol. , vol.37 , pp. 329-335
    • Lyles, G.A.1    Fitcpatrick, C.M.S.2
  • 260
    • 0021815710 scopus 로고
    • Vascular smooth muscle cells: A major source of the semicarbazide-sensitive amine oxidase of the rat aorta
    • Lyles, G. A. and Singh, I. (1985). Vascular smooth muscle cells: a major source of the semicarbazide-sensitive amine oxidase of the rat aorta. J. Pharm. Pharmacol. 37, 637-643.
    • (1985) J. Pharm. Pharmacol. , vol.37 , pp. 637-643
    • Lyles, G.A.1    Singh, I.2
  • 261
    • 0028182807 scopus 로고
    • Properties of mammalian tissue-bound semicarbazide-sensitive amine oxidase: Possible clues to its physiological function?
    • Lyles, G. A. (1994). Properties of mammalian tissue-bound semicarbazide-sensitive amine oxidase: Possible clues to its physiological function? J. Neural. Transm. 41, 387-396.
    • (1994) J. Neural. Transm. , vol.41 , pp. 387-396
    • Lyles, G.A.1
  • 262
    • 0029621215 scopus 로고
    • Substrate-specificity of mammalian tissue-bound semicarbazide-sensitive amine oxidase
    • Lyles, G. A. (1995). Substrate-specificity of mammalian tissue-bound semicarbazide-sensitive amine oxidase. Progr. Brain Res. 106, 293-303.
    • (1995) Progr. Brain Res. , vol.106 , pp. 293-303
    • Lyles, G.A.1
  • 263
    • 0029869337 scopus 로고    scopus 로고
    • Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: Biochemical, pharmacological and toxicological aspects
    • Lyles, G. A. (1996). Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: Biochemical, pharmacological and toxicological aspects. Int. J. Biochem. Cell Biol. 28, 259-274.
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 259-274
    • Lyles, G.A.1
  • 265
    • 0019776494 scopus 로고
    • Metabolism of acetyl derivatives of polyamines in cultured polyamine-deficient rat hepatoma cells
    • Mamont, P. S., Seiler, N., Siat, M., Joder-Ohlenbusch, A.-M. and Knödgen, B. (1981). Metabolism of acetyl derivatives of polyamines in cultured polyamine-deficient rat hepatoma cells. Med. Biol. 59, 347-353.
    • (1981) Med. Biol. , vol.59 , pp. 347-353
    • Mamont, P.S.1    Seiler, N.2    Siat, M.3    Joder-Ohlenbusch, A.-M.4    Knödgen, B.5
  • 266
    • 0027978954 scopus 로고
    • Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin
    • Mann, D. M., Romm, E. and Migliorini, M. (1994). Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin. J. Biol. Chem. 269, 23661-23667.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23661-23667
    • Mann, D.M.1    Romm, E.2    Migliorini, M.3
  • 267
    • 0023009428 scopus 로고
    • The condensation of chromatin and histone H1-depleted chromatin by spermine
    • Marquet, R., Colson, P. and Houssier, C. (1986). The condensation of chromatin and histone H1-depleted chromatin by spermine. J. Biomol. Struct. Dynam. 4, 205-218.
    • (1986) J. Biomol. Struct. Dynam. , vol.4 , pp. 205-218
    • Marquet, R.1    Colson, P.2    Houssier, C.3
  • 268
    • 0022919803 scopus 로고
    • Polyamine-DNA interactions: Possible site of new cancer chemotherapeutic intervention
    • Marton, L. J. and Feuerstein, B. G. (1986). Polyamine-DNA interactions: possible site of new cancer chemotherapeutic intervention. Pharmaceutical Res. 3, 311-317.
    • (1986) Pharmaceutical Res. , vol.3 , pp. 311-317
    • Marton, L.J.1    Feuerstein, B.G.2
  • 269
    • 0019876646 scopus 로고
    • Properties of spermidine N-acetyltransferase from livers of rats treated with carbon tetrachloride and its role in the conversion of spermidine into putrescine
    • Matsui, I., Wiegand, L. and Pegg, A. E. (1981). Properties of spermidine N-acetyltransferase from livers of rats treated with carbon tetrachloride and its role in the conversion of spermidine into putrescine. J. Biol. Chem. 256, 2454-2459.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2454-2459
    • Matsui, I.1    Wiegand, L.2    Pegg, A.E.3
  • 270
    • 0020465882 scopus 로고
    • Conversion of exogenous spermidine into putrescine after administration to rats
    • Matsui, I., Pösö, H. and Pegg, A. E. (1982). Conversion of exogenous spermidine into putrescine after administration to rats. Biochim. Biophys. Acta 719, 199-207.
    • (1982) Biochim. Biophys. Acta , vol.719 , pp. 199-207
    • Matsui, I.1    Pösö, H.2    Pegg, A.E.3
  • 272
    • 0018140325 scopus 로고
    • Kinetics of polyamine synthesis and turnover in mouse fibroblasts
    • McCormick, F. (1978). Kinetics of polyamine synthesis and turnover in mouse fibroblasts. Biochem. J. 174, 427-434.
    • (1978) Biochem. J. , vol.174 , pp. 427-434
    • McCormick, F.1
  • 273
    • 0013781611 scopus 로고
    • Human plasma monoamine oxidase. I. Purification and identification
    • McEwen, C. M. (1965). Human plasma monoamine oxidase. I. Purification and identification. J. Biol. Chem. 240, 2003-2010.
    • (1965) J. Biol. Chem. , vol.240 , pp. 2003-2010
    • McEwen, C.M.1
  • 274
    • 0022521983 scopus 로고
    • Effect of 1,3,6-triaminohexane and 1,4,7-triaminoheptane on growth and polyamine metabolism in SV-3T3 cells treated with 2-difluoromethylornithine
    • McGovern, K. A., Clark, R. S. and Pegg, A. E. (1986). Effect of 1,3,6-triaminohexane and 1,4,7-triaminoheptane on growth and polyamine metabolism in SV-3T3 cells treated with 2-difluoromethylornithine. J. Cell. Physiol. 127, 311-316.
    • (1986) J. Cell. Physiol. , vol.127 , pp. 311-316
    • McGovern, K.A.1    Clark, R.S.2    Pegg, A.E.3
  • 275
    • 0023040761 scopus 로고
    • Effects of polyamines on translation fidelity in vivo
    • McMurry, L. M. and Algranati, I. D. (1986). Effects of polyamines on translation fidelity in vivo. Eur. J. Biochem. 155, 383-390.
    • (1986) Eur. J. Biochem. , vol.155 , pp. 383-390
    • McMurry, L.M.1    Algranati, I.D.2
  • 276
    • 0017846283 scopus 로고
    • Diminished excretion of polyamines from BHK-21/cl3 cells exposed to methylglyoxal bis(guanylhydrazone)
    • Melvin, M. A. L. and Keir, H. M. (1978a). Diminished excretion of polyamines from BHK-21/cl3 cells exposed to methylglyoxal bis(guanylhydrazone). Biochem. J. 174, 349-352.
    • (1978) Biochem. J. , vol.174 , pp. 349-352
    • Melvin, M.A.L.1    Keir, H.M.2
  • 277
    • 0017883171 scopus 로고
    • Polyamine metabolism inBHK21/cl3 cells
    • Melvin, M. A. L. and Keir, H. M. (1978b). Polyamine metabolism inBHK21/cl3 cells. Exp. Cell. Res. 111, 231-236.
    • (1978) Exp. Cell. Res. , vol.111 , pp. 231-236
    • Melvin, M.A.L.1    Keir, H.M.2
  • 278
    • 0024460504 scopus 로고
    • Enhancement of mitogen-induced lymphocyte proliferation by some inhibitors of alkaline phosphatase and diamine oxidase
    • Metaye, T., Baudry, M. and Lalegerie, P. (1989). Enhancement of mitogen-induced lymphocyte proliferation by some inhibitors of alkaline phosphatase and diamine oxidase. Int. J. Immunopharmacol. 11, 629-636.
    • (1989) Int. J. Immunopharmacol. , vol.11 , pp. 629-636
    • Metaye, T.1    Baudry, M.2    Lalegerie, P.3
  • 279
    • 0017821358 scopus 로고
    • Bovine liver monoamine oxidase. A modified purification procedure and preliminary evidence for two subunits and one FAD
    • Minamiura, N. and Yasunobu, K. T. (1978). Bovine liver monoamine oxidase. A modified purification procedure and preliminary evidence for two subunits and one FAD. Arch. Biochem. Biophys. 189, 481-489.
    • (1978) Arch. Biochem. Biophys. , vol.189 , pp. 481-489
    • Minamiura, N.1    Yasunobu, K.T.2
  • 280
    • 0018897949 scopus 로고
    • Putrescine catabolism in rats given heparin or aminoguanidine
    • Missala, K. and Sourkes, T. L. (1980). Putrescine catabolism in rats given heparin or aminoguanidine. Eur. J. Pharmacol. 64, 307-311.
    • (1980) Eur. J. Pharmacol. , vol.64 , pp. 307-311
    • Missala, K.1    Sourkes, T.L.2
  • 281
    • 0013769989 scopus 로고
    • Purification of pig kidney diamine oxidase and its identity with histaminase
    • Mondovi, B., Rotilio, G., Finazzi, A. and Scioscia-Santoro, A. (1964). Purification of pig kidney diamine oxidase and its identity with histaminase. Biochem. J. 91, 408-415.
    • (1964) Biochem. J. , vol.91 , pp. 408-415
    • Mondovi, B.1    Rotilio, G.2    Finazzi, A.3    Scioscia-Santoro, A.4
  • 286
    • 0024148453 scopus 로고
    • The biological functions of amine oxidases and their reaction products: An overview
    • Mondovi, B., Riccio, P. and Agostinello, E. (1988). The biological functions of amine oxidases and their reaction products: an overview. Adv. Exp. Med. Biol. 250, 147-161.
    • (1988) Adv. Exp. Med. Biol. , vol.250 , pp. 147-161
    • Mondovi, B.1    Riccio, P.2    Agostinello, E.3
  • 289
    • 84987411013 scopus 로고
    • Polyamine oxidase in human pregnancy: A possible immunomodulatory agent
    • Morgan, D. M. L. (1981). Polyamine oxidase in human pregnancy: A possible immunomodulatory agent. Biochem. Soc. Transact. 9, 400-401.
    • (1981) Biochem. Soc. Transact. , vol.9 , pp. 400-401
    • Morgan, D.M.L.1
  • 290
    • 0019350050 scopus 로고
    • Radiochemical estimation of serum polyamine oxidase activity in human pregnancy
    • Morgan, D. M. L. and Illei, G. (1981). Radiochemical estimation of serum polyamine oxidase activity in human pregnancy. Med. Lab. Sci. 38, 49-56.
    • (1981) Med. Lab. Sci. , vol.38 , pp. 49-56
    • Morgan, D.M.L.1    Illei, G.2
  • 291
    • 0343261201 scopus 로고
    • Polyamine oxidation and human pregnancy
    • (Eds. Bachrach, U., Kaye, A. and Chayen, R.), Raven Press, New York, USA
    • Morgan, D. M. L. (1983). Polyamine oxidation and human pregnancy. In Adv. Polyamine Res. 4 (Eds. Bachrach, U., Kaye, A. and Chayen, R.), pp. 155-167, Raven Press, New York, USA.
    • (1983) Adv. Polyamine Res. , vol.4 , pp. 155-167
    • Morgan, D.M.L.1
  • 293
    • 0022512551 scopus 로고
    • 8-acetylspermidine, and magnesium: Determination from analysis of the broadening of thermal denaturation curves
    • 8-acetylspermidine, and magnesium: determination from analysis of the broadening of thermal denaturation curves. Arch. Biochem. Biophys. 246, 225-232.
    • (1986) Arch. Biochem. Biophys. , vol.246 , pp. 225-232
    • Morgan, J.E.1    Blankenship, J.W.2    Matthews, H.R.3
  • 295
    • 0023126357 scopus 로고
    • Oxidised polyamines and the growth of human vascular endothelial cells
    • Morgan, D. M. L. (1987b). Oxidised polyamines and the growth of human vascular endothelial cells. Biochem. J. 242, 347-352.
    • (1987) Biochem. J. , vol.242 , pp. 347-352
    • Morgan, D.M.L.1
  • 296
    • 0023657730 scopus 로고
    • Polyamines and acetylpolyamines increase the stability and alter the conformation of nucleosome core particles
    • Morgan, J. E., Blankenship, J. W. and Matthews, H. R. (1987). Polyamines and acetylpolyamines increase the stability and alter the conformation of nucleosome core particles. Biochemistry 26, 3643-3649.
    • (1987) Biochemistry , vol.26 , pp. 3643-3649
    • Morgan, J.E.1    Blankenship, J.W.2    Matthews, H.R.3
  • 297
    • 0030909369 scopus 로고    scopus 로고
    • Membrane amine oxidase cloning and identification as a major protein in the adipocyte plasma membrane
    • Morris, N. J., Ducret, A., Aebersold, R., Ross, S. A., Keller, S. R. and Lienhard, G. E. (1997). Membrane amine oxidase cloning and identification as a major protein in the adipocyte plasma membrane. J. Biol. Chem. 272, 9388-9392.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9388-9392
    • Morris, N.J.1    Ducret, A.2    Aebersold, R.3    Ross, S.A.4    Keller, S.R.5    Lienhard, G.E.6
  • 300
    • 0023663395 scopus 로고
    • Growth signal transduction: Rapid activaton of covalently bound ornithine decarboxylase during phosphatidylinositol breakdown
    • Mustelin, T., Pösö, H., Lapinjoki, S. P., Gynther, J. and Andersson, L. C. (1987). Growth signal transduction: Rapid activaton of covalently bound ornithine decarboxylase during phosphatidylinositol breakdown. Cell 49, 171-176.
    • (1987) Cell , vol.49 , pp. 171-176
    • Mustelin, T.1    Pösö, H.2    Lapinjoki, S.P.3    Gynther, J.4    Andersson, L.C.5
  • 301
    • 0027978741 scopus 로고
    • Modulation of lysyl oxidase activity toward peptidyl lysine by vicinal dicarboxylic amino acid residues
    • Nagan, N. and Kagan, H. M. (1994). Modulation of lysyl oxidase activity toward peptidyl lysine by vicinal dicarboxylic amino acid residues. J. Biol. Chem. 269, 22366-22371.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22366-22371
    • Nagan, N.1    Kagan, H.M.2
  • 303
    • 0028208355 scopus 로고
    • Light microscopic visualization of semicarbazide-sensitive amine oxidase (benzylamine oxidase) using a cerium method
    • Nakos, G. and Gossrau, R. (1994). Light microscopic visualization of semicarbazide-sensitive amine oxidase (benzylamine oxidase) using a cerium method. Folia Histochem. Cytobiolog. 32, 3-10.
    • (1994) Folia Histochem. Cytobiolog. , vol.32 , pp. 3-10
    • Nakos, G.1    Gossrau, R.2
  • 304
    • 0018761277 scopus 로고
    • An evaluation of three methods for the measurement of diamine oxidase (DAO) in amniotic fluid
    • Neufeld, E. and Chayen, R. (1979). An evaluation of three methods for the measurement of diamine oxidase (DAO) in amniotic fluid. Anal. Biochem. 96, 411-418.
    • (1979) Anal. Biochem. , vol.96 , pp. 411-418
    • Neufeld, E.1    Chayen, R.2
  • 305
    • 0028959708 scopus 로고
    • Putrescine level in blood from the rat portal vein is influenced by inhibition of diamine oxidase
    • Nilsson, B.-O. and Rosengren, E. (1995). Putrescine level in blood from the rat portal vein is influenced by inhibition of diamine oxidase. Acta Physiol. Scand. 153, 395-396.
    • (1995) Acta Physiol. Scand. , vol.153 , pp. 395-396
    • Nilsson, B.-O.1    Rosengren, E.2
  • 306
    • 0029826422 scopus 로고    scopus 로고
    • Inhibition of diamine oxidase promotes uptake of putrescine from rat small intestine
    • Nilsson, B.-O., Kochum, I. and Rosengren, E. (1996). Inhibition of diamine oxidase promotes uptake of putrescine from rat small intestine. Inflamm. Res. 45, 513-518.
    • (1996) Inflamm. Res. , vol.45 , pp. 513-518
    • Nilsson, B.-O.1    Kochum, I.2    Rosengren, E.3
  • 307
    • 0022655211 scopus 로고
    • Fetal calf serum-mediated toxicity of human polyamines to lymphocytes
    • Nishida, Y. and Miyamoto, T. (1986). Fetal calf serum-mediated toxicity of human polyamines to lymphocytes. Toxicol. Lett. 31, 203-209.
    • (1986) Toxicol. Lett. , vol.31 , pp. 203-209
    • Nishida, Y.1    Miyamoto, T.2
  • 308
    • 0020585734 scopus 로고
    • The role of polyamine biosynthesis in hemato-poietic precursor cell proliferation in mice
    • Niskanen, E., Kallio, A., McCann, P. P. and Baker, D. G. (1983). The role of polyamine biosynthesis in hemato-poietic precursor cell proliferation in mice. Blood 61, 740-745.
    • (1983) Blood , vol.61 , pp. 740-745
    • Niskanen, E.1    Kallio, A.2    McCann, P.P.3    Baker, D.G.4
  • 309
    • 0023597895 scopus 로고
    • Diamine oxidase is important in assessment of polyamine effects on hemopoietic cell proliferation in vitro
    • Niskanen, E. and Wharton, W. W. (1987). Diamine oxidase is important in assessment of polyamine effects on hemopoietic cell proliferation in vitro. In Vitro Cell. Developm. Biol. 23, 257-260.
    • (1987) In Vitro Cell. Developm. Biol. , vol.23 , pp. 257-260
    • Niskanen, E.1    Wharton, W.W.2
  • 310
    • 0028363143 scopus 로고
    • Diamine oxidase is the amilorid-binding protein and is inhibited by amilorid analogues
    • Novotny, W. F., Chassande, O., Baker, M., Lazdunski, M. and Barbry, P. (1994). Diamine oxidase is the amilorid-binding protein and is inhibited by amilorid analogues. J. Biol. Chem. 269, 9921-9925.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9921-9925
    • Novotny, W.F.1    Chassande, O.2    Baker, M.3    Lazdunski, M.4    Barbry, P.5
  • 311
    • 0001155678 scopus 로고
    • Determination of diamine oxidase activity by liquid scintillation counting
    • Okuyama, T. and Kobayashi, Y. (1961). Determination of diamine oxidase activity by liquid scintillation counting. Arch. Biochem. Biophys. 95, 242-250.
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 242-250
    • Okuyama, T.1    Kobayashi, Y.2
  • 312
    • 84990557232 scopus 로고
    • Progressive increase in polyamine levels in 9l cells in vitro during the cell cycle: Comparison between cells isolated by centrifugal elutriation and cells grown in synchrony
    • Oredsson, S. M., Gray, J. W. and Marton, L. J. (1984). Progressive increase in polyamine levels in 9L cells in vitro during the cell cycle: comparison between cells isolated by centrifugal elutriation and cells grown in synchrony. Cell Tissue Kinet. 17, 437-444.
    • (1984) Cell Tissue Kinet. , vol.17 , pp. 437-444
    • Oredsson, S.M.1    Gray, J.W.2    Marton, L.J.3
  • 313
    • 0028016495 scopus 로고
    • Ornithine decarboxylase is a mediator of c-myc induced apoptosis
    • Packham, G. and Cleveland, J. L. (1994). Ornithine decarboxylase is a mediator of c-Myc induced apoptosis. Mol. Cell. Biol. 14, 5741-5747.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5741-5747
    • Packham, G.1    Cleveland, J.L.2
  • 314
    • 0023893063 scopus 로고
    • Polyamine metabolism and interconversion in NIH 3T3 and ras-transfected NIH 3T3 cells
    • Pakala, P., Kreisel, M. and Bachrach, U. (1988). Polyamine metabolism and interconversion in NIH 3T3 and ras-transfected NIH 3T3 cells. Cancer Res. 48, 3336-3340.
    • (1988) Cancer Res. , vol.48 , pp. 3336-3340
    • Pakala, P.1    Kreisel, M.2    Bachrach, U.3
  • 315
    • 0024368618 scopus 로고
    • Polyamine oxidation, programmed cell death, and regulation of melanoma in the murine embryonic limb
    • Parchment, R. E. and Pierce, G. B. (1989). Polyamine oxidation, programmed cell death, and regulation of melanoma in the murine embryonic limb. Cancer Res. 49, 6680-6686.
    • (1989) Cancer Res. , vol.49 , pp. 6680-6686
    • Parchment, R.E.1    Pierce, G.B.2
  • 317
    • 0025967971 scopus 로고
    • Specific detection of quinoproteins by redox-cycling staining
    • Paz, M. A., Flückiger, R., Boak, A., Kagan, H. M. and Gallop, P. M. (1991). Specific detection of quinoproteins by redox-cycling staining. J. Biol. Chem. 266, 689-692.
    • (1991) J. Biol. Chem. , vol.266 , pp. 689-692
    • Paz, M.A.1    Flückiger, R.2    Boak, A.3    Kagan, H.M.4    Gallop, P.M.5
  • 320
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy
    • Pegg, A. E. (1988). Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy. Cancer Res. 48, 759-774.
    • (1988) Cancer Res. , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 321
    • 0029012726 scopus 로고
    • Lactoferrin down-modulates the activity of the granulocyte macrophage colony-stimulating factor promoter in interleukin-1β-stimulated cells
    • Penco, S., Pastorino, S., Bianchi-Scarra, G. and Garré, C. (1995). Lactoferrin down-modulates the activity of the granulocyte macrophage colony-stimulating factor promoter in interleukin-1β-stimulated cells. J. Biol. Chem. 270, 12263-12268.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12263-12268
    • Penco, S.1    Pastorino, S.2    Bianchi-Scarra, G.3    Garré, C.4
  • 322
    • 0024384639 scopus 로고
    • Polyamine-mediated control of mammalian S-adenosyl-L-methionine decarboxylase expression: Effects on the content and translational efficiency of the mRNA
    • Persson, L., Stjernborg, E., Holm, I. and Heby, O. (1989). Polyamine-mediated control of mammalian S-adenosyl-L-methionine decarboxylase expression: effects on the content and translational efficiency of the mRNA. Biochem. Biophys. Res. Commun. 160, 1196-1202.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 1196-1202
    • Persson, L.1    Stjernborg, E.2    Holm, I.3    Heby, O.4
  • 323
    • 0022513621 scopus 로고
    • Ornithine decarboxylase, transglutaminase, diamine oxidase and total diamines and polyamines in maternal liver and kidney throughout rat pregnancy
    • Piacentini, M., Sartori, C., Beninati, S., Bargagli, A. M. and Cerü-Argento, M. P. (1986). Ornithine decarboxylase, transglutaminase, diamine oxidase and total diamines and polyamines in maternal liver and kidney throughout rat pregnancy. Biochem. J. 234, 435-440.
    • (1986) Biochem. J. , vol.234 , pp. 435-440
    • Piacentini, M.1    Sartori, C.2    Beninati, S.3    Bargagli, A.M.4    Cerü-Argento, M.P.5
  • 325
    • 0025760425 scopus 로고
    • Hydrogen peroxide as a mediator of programmed cell death in the blastocyst
    • Pierce, G. B., Parchment, R. E. and Lewellyn, A. L. (1991). Hydrogen peroxide as a mediator of programmed cell death in the blastocyst. Differentiation 46, 181-186.
    • (1991) Differentiation , vol.46 , pp. 181-186
    • Pierce, G.B.1    Parchment, R.E.2    Lewellyn, A.L.3
  • 326
    • 0029968417 scopus 로고    scopus 로고
    • Phosphorylation of okazaki-like DNA fragments in mammalian cells and role of polyamines in the processing of this DNA
    • Pohjanpelto, P. and Hölttä, E. (1996). Phosphorylation of Okazaki-like DNA fragments in mammalian cells and role of polyamines in the processing of this DNA. EMBO J. 15, 1193-1200.
    • (1996) EMBO J. , vol.15 , pp. 1193-1200
    • Pohjanpelto, P.1    Hölttä, E.2
  • 327
    • 0021094476 scopus 로고
    • Spermidine requirement for cell proliferation in eucaryotic cells: Structural specificity and quantitation
    • Porter, C. W. and Bergeron, R. J. (1983). Spermidine requirement for cell proliferation in eucaryotic cells: structural specificity and quantitation. Science 219, 1083-1085.
    • (1983) Science , vol.219 , pp. 1083-1085
    • Porter, C.W.1    Bergeron, R.J.2
  • 328
    • 0023793499 scopus 로고
    • Properties of semicarbazide-sensitive amine oxidase in human umbilical artery
    • Precious, E. and Lyles, G. A. (1988). Properties of semicarbazide-sensitive amine oxidase in human umbilical artery. J. Pharm. Pharmacol. 40, 627-633.
    • (1988) J. Pharm. Pharmacol. , vol.40 , pp. 627-633
    • Precious, E.1    Lyles, G.A.2
  • 329
    • 0023869739 scopus 로고
    • Deamination of methylamine by semicarbazide-sensitive amine oxidase in human umbilical artery and rat aorta
    • Precious, E., Gunn, C. E. and Lyles, G. A. (1988). Deamination of methylamine by semicarbazide-sensitive amine oxidase in human umbilical artery and rat aorta. Biochem. Pharmacol. 37, 707-713.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 707-713
    • Precious, E.1    Gunn, C.E.2    Lyles, G.A.3
  • 330
    • 0029856089 scopus 로고    scopus 로고
    • Evidence of a semicarbazide-sensitive amine oxidase activity in guinea pig tissues
    • Puliti, M., Cambi, S. and Buffoni, F. (1996). Evidence of a semicarbazide-sensitive amine oxidase activity in guinea pig tissues. Comp. Biochem. Physiol. 115B, 159-165.
    • (1996) Comp. Biochem. Physiol. , vol.115 B , pp. 159-165
    • Puliti, M.1    Cambi, S.2    Buffoni, F.3
  • 331
    • 0019804431 scopus 로고
    • Differences between tissues in response of s-adenosylmethionine decarboxylase to administration of polyamines
    • Pösö, H. and Pegg, A. E. (1981). Differences between tissues in response of S-adenosylmethionine decarboxylase to administration of polyamines. Biochem. J. 200, 629-637.
    • (1981) Biochem. J. , vol.200 , pp. 629-637
    • Pösö, H.1    Pegg, A.E.2
  • 332
    • 0025340505 scopus 로고
    • Delineation between T and B suppressive molecules from human seminal plasma: II. Spermine is the major suppressor of T-lymphocytes
    • Quan, C. P., Roux, C., Pillot, J. and Bouvet, J.-P. (1990). Delineation between T and B suppressive molecules from human seminal plasma: II. Spermine is the major suppressor of T-lymphocytes in vitro. Am. J. Reprod. Immunol. 22, 64-69.
    • (1990) In Vitro. Am. J. Reprod. Immunol. , vol.22 , pp. 64-69
    • Quan, C.P.1    Roux, C.2    Pillot, J.3    Bouvet, J.-P.4
  • 333
    • 0014863759 scopus 로고
    • Serum β-aminopropionaldehyde: Identification and origin
    • Quash, G. and Taylor, D. R. (1970). Serum β-aminopropionaldehyde: identification and origin. Clin. Chim. Acta 30, 17-23.
    • (1970) Clin. Chim. Acta , vol.30 , pp. 17-23
    • Quash, G.1    Taylor, D.R.2
  • 334
    • 0023284951 scopus 로고
    • Malondialdehyde production from spermine by homogenates of normal and transformed cells
    • Quash, G., Ripoll, H., Gazzalo, L., Doutheau, A., Saba, A. and Gore, J. (1987). Malondialdehyde production from spermine by homogenates of normal and transformed cells. Biochimie 69, 101-108.
    • (1987) Biochimie , vol.69 , pp. 101-108
    • Quash, G.1    Ripoll, H.2    Gazzalo, L.3    Doutheau, A.4    Saba, A.5    Gore, J.6
  • 336
    • 0026060802 scopus 로고
    • Semicarbazide-sensitive amine oxidase activity (SSAO) of rat epididymal white adipose tissue
    • Raimondi, L., Pirisino, R., Ignesti, G., Capecchi, S., Banchelli, G. and Buffoni, F. (1991). Semicarbazide-sensitive amine oxidase activity (SSAO) of rat epididymal white adipose tissue. Biochem. Pharmaol. 41, 467-470.
    • (1991) Biochem. Pharmaol. , vol.41 , pp. 467-470
    • Raimondi, L.1    Pirisino, R.2    Ignesti, G.3    Capecchi, S.4    Banchelli, G.5    Buffoni, F.6
  • 339
    • 0016687709 scopus 로고
    • Physiology of the natural polyamines putrescine, spermidine and spermine
    • Raina, A. and Jänne, J. (1975). Physiology of the natural polyamines putrescine, spermidine and spermine. Med. Biol. 53, 121-147.
    • (1975) Med. Biol. , vol.53 , pp. 121-147
    • Raina, A.1    Jänne, J.2
  • 340
    • 0022551097 scopus 로고
    • Absence of diamine oxidase from rabbit and rat lungs
    • Rao, S. B., Rao, K. S. P. and Mehendale, H. M. (1986). Absence of diamine oxidase from rabbit and rat lungs. Biochem. J. 234, 733-736.
    • (1986) Biochem. J. , vol.234 , pp. 733-736
    • Rao, S.B.1    Rao, K.S.P.2    Mehendale, H.M.3
  • 341
    • 0020009861 scopus 로고
    • Diamine oxidase from pig kidney: New purification method and amino acid composition
    • Rinaldi, A., Vecchim, P. and Floris, G. (1982). Diamine oxidase from pig kidney: New purification method and amino acid composition. Preparative Biochem. 12, 11-28.
    • (1982) Preparative Biochem. , vol.12 , pp. 11-28
    • Rinaldi, A.1    Vecchim, P.2    Floris, G.3
  • 344
    • 0021238429 scopus 로고
    • Localisation of histaminase to the specific granule of the human neutrophil
    • Ringel, E. W., Soter, N. A. and Austen, K. F. (1984). Localisation of histaminase to the specific granule of the human neutrophil. Immunology 52, 649-658.
    • (1984) Immunology , vol.52 , pp. 649-658
    • Ringel, E.W.1    Soter, N.A.2    Austen, K.F.3
  • 345
    • 0014084155 scopus 로고
    • Preparation of starch gel zymograms: Peroxide-producing enzymes and ceruloplasmin
    • Robinson, J. C. and Lee, G. (1967). Preparation of starch gel zymograms: Peroxide-producing enzymes and ceruloplasmin. Arch. Biochem. Biophys. 120, 428-433.
    • (1967) Arch. Biochem. Biophys. , vol.120 , pp. 428-433
    • Robinson, J.C.1    Lee, G.2
  • 346
    • 0022416633 scopus 로고
    • Binding of diamine oxidase to rat and guinea pig microvascular endothelial cells
    • Robinson-White, A., Baylin, S. B., Olivecrona, T. and Beaven, M. A. (1985). Binding of diamine oxidase to rat and guinea pig microvascular endothelial cells. J. Clin. Invest. 76, 93-100.
    • (1985) J. Clin. Invest. , vol.76 , pp. 93-100
    • Robinson-White, A.1    Baylin, S.B.2    Olivecrona, T.3    Beaven, M.A.4
  • 347
    • 0018399535 scopus 로고
    • Excretion of polyamines by the pregnant rat following inhibition of diamine oxidase
    • Rojansky, N., Neufeld, E. and Chayen, R. (1979). Excretion of polyamines by the pregnant rat following inhibition of diamine oxidase. Biochim. Biophys. Acta 586, 1-9.
    • (1979) Biochim. Biophys. Acta , vol.586 , pp. 1-9
    • Rojansky, N.1    Neufeld, E.2    Chayen, R.3
  • 348
    • 0023734857 scopus 로고
    • Polyamine oxidase activity in serum of cancer patients and healthy subjects
    • Romano, M. and Bonelli, P. (1988). Polyamine oxidase activity in serum of cancer patients and healthy subjects. Tumori 74, 397-399.
    • (1988) Tumori , vol.74 , pp. 397-399
    • Romano, M.1    Bonelli, P.2
  • 349
    • 0019776020 scopus 로고
    • Polyamine metabolism as related to growth and hormones
    • Rosengren, E., Henningson, A.-Ch., Henningson, S. and Persson, L. (1981). Polyamine metabolism as related to growth and hormones. Med. Biol. 59, 320-326.
    • (1981) Med. Biol. , vol.59 , pp. 320-326
    • Rosengren, E.1    Henningson, A.-Ch.2    Henningson, S.P.L.3
  • 350
    • 0016775874 scopus 로고
    • Multiple forms of amine oxidase in perfused rabbit lung
    • Roth, J. A. and Gillis, C. N. (1975). Multiple forms of amine oxidase in perfused rabbit lung. J. Pharmacol. Exp. Therap. 194, 537-544.
    • (1975) J. Pharmacol. Exp. Therap. , vol.194 , pp. 537-544
    • Roth, J.A.1    Gillis, C.N.2
  • 351
    • 0015222817 scopus 로고
    • Connective tissue amine oxidase. I. Purification of bovine aorta amine oxidase and its comparison with plasma amine oxidase
    • Rucker, R. B. and O'dell, B. L. (1971). Connective tissue amine oxidase. I. Purification of bovine aorta amine oxidase and its comparison with plasma amine oxidase. Biochim. Biophys. Acta. 235, 32-43.
    • (1971) Biochim. Biophys. Acta. , vol.235 , pp. 32-43
    • Rucker, R.B.1    O'dell, B.L.2
  • 352
    • 0022620325 scopus 로고
    • Influence of several aldehyde dehydrogenase and aldehyde reductase inhibitors on diamine oxidase in rat brain
    • Ruggieri, P., Saija, A., Costa, G. and Caputi, A. P. (1986). Influence of several aldehyde dehydrogenase and aldehyde reductase inhibitors on diamine oxidase in rat brain. Res. Commun. Chem. Pathol. Pharmacol. 51, 205-209.
    • (1986) Res. Commun. Chem. Pathol. Pharmacol. , vol.51 , pp. 205-209
    • Ruggieri, P.1    Saija, A.2    Costa, G.3    Caputi, A.P.4
  • 353
    • 0006048599 scopus 로고
    • Regulation of the cell cycle by polyamines in normal and transformed fibroblasts
    • (Eds. Campbell et al.), Raven Press, New York
    • Rupniak, H. T. and Paul, D. (1978). Regulation of the cell cycle by polyamines in normal and transformed fibroblasts. Adv. Polyamine Res. Vol. 1 (Eds. Campbell et al.), pp. 117-126, Raven Press, New York.
    • (1978) Adv. Polyamine Res. , vol.1 , pp. 117-126
    • Rupniak, H.T.1    Paul, D.2
  • 354
    • 0027368071 scopus 로고
    • Induction and function of vascular adhesion protein-1 at sites of inflammation
    • Salmi, M., Kalimo, K. and Jalkanen, S. (1993). Induction and function of vascular adhesion protein-1 at sites of inflammation. J. Exp. Med. 178, 2255-2260.
    • (1993) J. Exp. Med. , vol.178 , pp. 2255-2260
    • Salmi, M.1    Kalimo, K.2    Jalkanen, S.3
  • 355
    • 0030057684 scopus 로고    scopus 로고
    • Human vascular adhesion protein 1 (VAP-I) is a unique sialoglycoprotein that mediates carbohydrate-dependent binding of lymphocytes to endothelial cells
    • Salmi, M. and Jalkanen, S. (1996). Human vascular adhesion protein 1 (VAP-I) is a unique sialoglycoprotein that mediates carbohydrate-dependent binding of lymphocytes to endothelial cells. J. Exp. Med. 183, 569-579.
    • (1996) J. Exp. Med. , vol.183 , pp. 569-579
    • Salmi, M.1    Jalkanen, S.2
  • 356
    • 0032101962 scopus 로고    scopus 로고
    • The role of two distinct endothelial molecules, vascular adhesion protein-1 and peripheral lymph node adressin, in the binding of lymphocyte subsets to human lymph nodes
    • Salmi, M., Hellman, J. and Jalkanen, S. (1998). The role of two distinct endothelial molecules, vascular adhesion protein-1 and peripheral lymph node adressin, in the binding of lymphocyte subsets to human lymph nodes. J. Immunol. 160, 5629-5636.
    • (1998) J. Immunol. , vol.160 , pp. 5629-5636
    • Salmi, M.1    Hellman, J.2    Jalkanen, S.3
  • 357
  • 358
    • 0023718220 scopus 로고
    • Compensatory route of spermidine acetylation and oxidation can supply sufficient putrescine for hepatic DNA synthesis at an early stage after partial hepatectomy in diaminopropane-treatedrats
    • Sato, Y. and Fujiwara, K. (1988). Compensatory route of spermidine acetylation and oxidation can supply sufficient putrescine for hepatic DNA synthesis at an early stage after partial hepatectomy in diaminopropane-treatedrats. J. Biochem. 104, 98-101.
    • (1988) J. Biochem. , vol.104 , pp. 98-101
    • Sato, Y.1    Fujiwara, K.2
  • 359
    • 0020020939 scopus 로고
    • Polyamines in mammalian tumors. Part I
    • Scalabrino, G. and Ferioli, M. E. (1981). Polyamines in mammalian tumors. Part I. Adv. Cancer Res. 36, 1-102.
    • (1981) Adv. Cancer Res. , vol.36 , pp. 1-102
    • Scalabrino, G.1    Ferioli, M.E.2
  • 360
    • 0020020939 scopus 로고
    • Polyamines in mammalian tumors. Part II
    • Scalabrino, G. and Ferioli, M. E. (1982). Polyamines in mammalian tumors. Part II. Adv. Cancer Res. 36, 1-102.
    • (1982) Adv. Cancer Res. , vol.36 , pp. 1-102
    • Scalabrino, G.1    Ferioli, M.E.2
  • 361
    • 0021284677 scopus 로고
    • Polyamines in mammalian aging: An oncological problem too?
    • Scalabrino, G. and Ferioli, M. E. (1984). Polyamines in mammalian aging: an oncological problem too? A review. Mech. Ageing Developm. 26, 149-164.
    • (1984) A Review. Mech. Ageing Developm. , vol.26 , pp. 149-164
    • Scalabrino, G.1    Ferioli, M.E.2
  • 364
    • 0001267090 scopus 로고
    • The importance of both synthesis and degradation in the control of arginase levels in rat liver
    • Schimke, R. T. (1964). The importance of both synthesis and degradation in the control of arginase levels in rat liver. J. Biol. Chem. 239, 3808-3817.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3808-3817
    • Schimke, R.T.1
  • 365
    • 0024411864 scopus 로고
    • Spermidine level and protein synthesis are coregulated in non-proliferating hepatocytes
    • Schulz, W. A., Gebhardt, R. and Mecke, D. (1989). Spermidine level and protein synthesis are coregulated in non-proliferating hepatocytes. Biol. Chem. Hoppe-Zeyler 370, 729-736.
    • (1989) Biol. Chem. Hoppe-Zeyler , vol.370 , pp. 729-736
    • Schulz, W.A.1    Gebhardt, R.2    Mecke, D.3
  • 366
    • 0028918616 scopus 로고
    • Determination of the activity of diamine oxidase in extremely small tissue samples
    • Schwelberger, H. G., Klocker, J., Sattler, J. and Bodner, E. (1995a). Determination of the activity of diamine oxidase in extremely small tissue samples. Inflamm. Res. 44, Suppl. 1, S94-S95.
    • (1995) Inflamm. Res. , vol.44 , Issue.SUPPL. 1
    • Schwelberger, H.G.1    Klocker, J.2    Sattler, J.3    Bodner, E.4
  • 368
    • 0029919318 scopus 로고    scopus 로고
    • Purification of human intestinal diamine oxidase
    • Schwelberger, H. G., Sattler, J. and Bodner, E. (1996). Purification of human intestinal diamine oxidase. Inflamm. Res. 45, suppl. 1, S50-S51.
    • (1996) Inflamm. Res. , vol.45 , Issue.SUPPL. 1
    • Schwelberger, H.G.1    Sattler, J.2    Bodner, E.3
  • 369
    • 0030957182 scopus 로고    scopus 로고
    • Purification and characterization of diamine oxidase from porcine kidney and intestine
    • Schwelberger, H. G. and Bodner, E. (1997). Purification and characterization of diamine oxidase from porcine kidney and intestine. Biochim. Biophys. Acta 1340, 152-164.
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 152-164
    • Schwelberger, H.G.1    Bodner, E.2
  • 370
    • 0016289107 scopus 로고
    • Putrescine catabolism in mammalian brain
    • Seiler, N. and Al-Therib, M. J. (1974). Putrescine catabolism in mammalian brain. Biochem. J. 144, 29-35.
    • (1974) Biochem. J. , vol.144 , pp. 29-35
    • Seiler, N.1    Al-Therib, M.J.2
  • 371
    • 0016700339 scopus 로고
    • 4-aminobutyrate in mammalian putrescine metabolism
    • Seiler, N. and Eichentopf, B. (1975). 4-Aminobutyrate in mammalian putrescine metabolism. Biochem. J. 152, 201-210.
    • (1975) Biochem. J. , vol.152 , pp. 201-210
    • Seiler, N.1    Eichentopf, B.2
  • 372
    • 0019271015 scopus 로고
    • On the role of gaba invertebrate polyamine metabolism
    • Seiler, N. (1980). On the role of gaba invertebrate polyamine metabolism. Physiol. Chem. Physics 12, 411-429.
    • (1980) Physiol. Chem. Physics , vol.12 , pp. 411-429
    • Seiler, N.1
  • 374
    • 0019771417 scopus 로고
    • Interconversion, catabolism and elimination of the polyamines
    • Seiler, N., Bolkenius, F. N. and Rennert, O. M. (1981). Interconversion, catabolism and elimination of the polyamines. Med. Biol. 59, 334-346.
    • (1981) Med. Biol. , vol.59 , pp. 334-346
    • Seiler, N.1    Bolkenius, F.N.2    Rennert, O.M.3
  • 375
    • 0022091957 scopus 로고
    • Polyamine metabolism and polyamine excretion in normal and tumor bearing rodents
    • Seiler, N., Knödgen, B. and Bartholeyns, J. (1985a). Polyamine metabolism and polyamine excretion in normal and tumor bearing rodents. Anticancer Res. 5, 371-378.
    • (1985) Anticancer Res. , vol.5 , pp. 371-378
    • Seiler, N.1    Knödgen, B.2    Bartholeyns, J.3
  • 376
    • 0021920139 scopus 로고
    • The influence of catabolic reactions on polyamine excretion
    • Seiler, N., Bolkenius, N. and Knödgen, B. (1985b). The influence of catabolic reactions on polyamine excretion. Biochem J. 225, 219-226.
    • (1985) Biochem J. , vol.225 , pp. 219-226
    • Seiler, N.1    Bolkenius, N.2    Knödgen, B.3
  • 377
    • 0002303198 scopus 로고
    • Biochemical significance of inhibition of polyamine oxidase
    • (eds., Selmeci, L., Brosnan, M. E. and Seiler, N.), Akademiai Kiado, Budapest, Hungary.
    • Seiler, N., Bolkenius, F. N., Bey, P., Mamont, P. S. and Danzin, C. (1985c). Biochemical significance of inhibition of polyamine oxidase. In Recent progress in polyamine research (eds., Selmeci, L., Brosnan, M. E. and Seiler, N.), pp. 305-319, Akademiai Kiado, Budapest, Hungary.
    • (1985) Recent Progress in Polyamine Research , pp. 305-319
    • Seiler, N.1    Bolkenius, F.N.2    Bey, P.3    Mamont, P.S.4    Danzin, C.5
  • 378
    • 0023053502 scopus 로고
    • Polyamines
    • Seiler, N. (1986). Polyamines. J. Chr. 379, 167-176.
    • (1986) J. Chr. , vol.379 , pp. 167-176
    • Seiler, N.1
  • 379
    • 0023620631 scopus 로고
    • Functions of polyamine acetylation
    • Seiler, N. (1987). Functions of polyamine acetylation. Can. J. Physiol. Pharmacol. 65, 2024-2035.
    • (1987) Can. J. Physiol. Pharmacol. , vol.65 , pp. 2024-2035
    • Seiler, N.1
  • 380
    • 0023904365 scopus 로고
    • Regulation of cellular polyamines in mammals
    • Seiler, N. and Heby, O. (1988). Regulation of cellular polyamines in mammals. Acta. Biochim. Biophys. Hung. 23, 1-36.
    • (1988) Acta. Biochim. Biophys. Hung. , vol.23 , pp. 1-36
    • Seiler, N.1    Heby, O.2
  • 381
    • 0025298549 scopus 로고
    • Polyamine transport in mammalian cells
    • Seiler, N. and Dezeure, F. (1990). Polyamine transport in mammalian cells. Int. J. Biochem. 22, 211-218.
    • (1990) Int. J. Biochem. , vol.22 , pp. 211-218
    • Seiler, N.1    Dezeure, F.2
  • 382
    • 0029610668 scopus 로고
    • Polyamine oxidase, properties and functions
    • Seiler, N. (1995). Polyamine oxidase, properties and functions. Progr. Brain Res. 106, 333-344.
    • (1995) Progr. Brain Res. , vol.106 , pp. 333-344
    • Seiler, N.1
  • 383
    • 0019433186 scopus 로고
    • Diamine oxidase activity in regenerating rat liver and in 4-dimethyiaminoazobenzene-induced and yoshida AH 130 hepatomas
    • Sessa, A., Desiderio, M. A., Baizini, M. and Perin, A. (1981). Diamine oxidase activity in regenerating rat liver and in 4-dimethyIaminoazobenzene-induced and Yoshida AH 130 hepatomas. Cancer Res. 41, 1929-1934.
    • (1981) Cancer Res. , vol.41 , pp. 1929-1934
    • Sessa, A.1    Desiderio, M.A.2    Baizini, M.3    Perin, A.4
  • 384
    • 0023181769 scopus 로고
    • Effect of acute ethanol administration on diamine oxidase activity in maternal, embryonal and fetal tissues
    • Sessa, A., Desiderio, M. A. and Perin, A. (1987). Effect of acute ethanol administration on diamine oxidase activity in maternal, embryonal and fetal tissues. Agents and Actions 21, 49-53.
    • (1987) Agents and Actions , vol.21 , pp. 49-53
    • Sessa, A.1    Desiderio, M.A.2    Perin, A.3
  • 385
    • 0028172748 scopus 로고
    • Diamine oxidase in relation to diamine and polyamine metabolism
    • Sessa, A. and Perin, A. (1994). Diamine oxidase in relation to diamine and polyamine metabolism. Agents and Actions 43, 69-77.
    • (1994) Agents and Actions , vol.43 , pp. 69-77
    • Sessa, A.1    Perin, A.2
  • 386
    • 0028998328 scopus 로고
    • Diamine and polyamine oxidase activities in phytohaemagglutinin-induced growth of rat small intestine
    • Sessa, A., Tunici, P., Ewen, S. W. B., Grant, G., Pusztai, A., Bardocz, S. and Perin, A. (1995). Diamine and polyamine oxidase activities in phytohaemagglutinin-induced growth of rat small intestine. Biochim. Biophys. Acta 1244, 198-202.
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 198-202
    • Sessa, A.1    Tunici, P.2    Ewen, S.W.B.3    Grant, G.4    Pusztai, A.5    Bardocz, S.6    Perin, A.7
  • 387
    • 0023711997 scopus 로고
    • The glycoprotein nature of pig kidney diamine oxidase
    • Shah, M. A. and Ali, R. (1988). The glycoprotein nature of pig kidney diamine oxidase. Biochem. J. 253, 103-107.
    • (1988) Biochem. J. , vol.253 , pp. 103-107
    • Shah, M.A.1    Ali, R.2
  • 388
    • 0024520337 scopus 로고
    • Role of disulfides in biological activity and conformational stability of pig kidney diamine oxidase: Evidence for two disulfide states
    • Shah, M. A. and Ali, R. (1989). Role of disulfides in biological activity and conformational stability of pig kidney diamine oxidase: Evidence for two disulfide states. Biochem. Int. 1, 59-69.
    • (1989) Biochem. Int. , vol.1 , pp. 59-69
    • Shah, M.A.1    Ali, R.2
  • 389
    • 0017624709 scopus 로고
    • Localisation of histaminase (diamine oxidase) in rat small intestinal mucosa: Site of release by heparin
    • Shakir, K. M., Margolis, S. and Baylin, S. B. (1977). Localisation of histaminase (diamine oxidase) in rat small intestinal mucosa: Site of release by heparin. Biochem. Pharmacol. 26, 2343-2347.
    • (1977) Biochem. Pharmacol. , vol.26 , pp. 2343-2347
    • Shakir, K.M.1    Margolis, S.2    Baylin, S.B.3
  • 393
    • 0028305650 scopus 로고
    • Modification of the catalytic properties of diamine oxidase (DAO) by reducing agents
    • Silva, I. J., Azevedo, M. S. and Manso, C. F. (1994). Modification of the catalytic properties of diamine oxidase (DAO) by reducing agents. Biochem. Soc. Trans. 22, 222S.
    • (1994) Biochem. Soc. Trans. , vol.22
    • Silva, I.J.1    Azevedo, M.S.2    Manso, C.F.3
  • 394
    • 0022899164 scopus 로고
    • Role of ornithine decarboxylase and the polyamines in nervous system development: A review
    • Slotkin, T. A. and Bartolome, J. (1986). Role of ornithine decarboxylase and the polyamines in nervous system development: A review. Brain Res. Bull. 17, 307-320.
    • (1986) Brain Res. Bull. , vol.17 , pp. 307-320
    • Slotkin, T.A.1    Bartolome, J.2
  • 395
    • 0023986196 scopus 로고
    • Polyamine-DNA interactions, condensation of chromatin and naked DNA
    • Smimov, I. V., Dimitrov, S. I. and Makarov, V. L. (1988). Polyamine-DNA interactions, condensation of chromatin and naked DNA. J. Biomol. Struct. Dynam. 5, 1149-1161.
    • (1988) J. Biomol. Struct. Dynam. , vol.5 , pp. 1149-1161
    • Smimov, I.V.1    Dimitrov, S.I.2    Makarov, V.L.3
  • 396
    • 0014078176 scopus 로고
    • The purification and properties of placental histaminase
    • Smith, J. K. (1967). The purification and properties of placental histaminase. Biochem. J. 103, 110-119.
    • (1967) Biochem. J. , vol.103 , pp. 110-119
    • Smith, J.K.1
  • 397
    • 0020966588 scopus 로고
    • Inhibition of cells in culture by polyamines does not depend on the presence of ruminant serum
    • Smith, C. J., Maschler, R., Maurer, H. R. and Allen, J. C. (1983). Inhibition of cells in culture by polyamines does not depend on the presence of ruminant serum. Cell Tissue Kinet. 16, 269-276.
    • (1983) Cell Tissue Kinet. , vol.16 , pp. 269-276
    • Smith, C.J.1    Maschler, R.2    Maurer, H.R.3    Allen, J.C.4
  • 398
    • 0021959636 scopus 로고
    • Inhibition of cell proliferation by polyamines does not depend on the cytytoxicity of acrolein
    • Smith, C. J., Hussain, J. I. and Allen, J. C. (1985). Inhibition of cell proliferation by polyamines does not depend on the cytytoxicity of acrolein. Biochem. Soc. Transact. 13, 326-329.
    • (1985) Biochem. Soc. Transact. , vol.13 , pp. 326-329
    • Smith, C.J.1    Hussain, J.I.2    Allen, J.C.3
  • 399
    • 0024148185 scopus 로고
    • The di- and polyamine oxidases of plants
    • Smith, T. A. and Barker, J. H. A. (1988). The di- and polyamine oxidases of plants. Adv. Exp. Med. Biol. 250, 573-587.
    • (1988) Adv. Exp. Med. Biol. , vol.250 , pp. 573-587
    • Smith, T.A.1    Barker, J.H.A.2
  • 400
    • 0032490640 scopus 로고    scopus 로고
    • Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule
    • Smith, D. J., Salmi, M., Bono, P., Leu, T. and Jalkanen, S. (1998). Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J. Exp. Med. 188, 17-27.
    • (1998) J. Exp. Med. , vol.188 , pp. 17-27
    • Smith, D.J.1    Salmi, M.2    Bono, P.3    Leu, T.4    Jalkanen, S.5
  • 401
    • 0014258327 scopus 로고
    • Regulation of histidine decarboxylase in rat stomach by gastrin: The effect of inhibitors of protein synthesis
    • Snyder, S. H. and Epps, L. (1968). Regulation of histidine decarboxylase in rat stomach by gastrin: The effect of inhibitors of protein synthesis. Mol. Pharmacol. 4, 187-195.
    • (1968) Mol. Pharmacol. , vol.4 , pp. 187-195
    • Snyder, S.H.1    Epps, L.2
  • 403
    • 0013931856 scopus 로고
    • Serial measurements of plasma diamine oxidase (DAO) during normal human pregnancy by an improved method
    • Southren, A. L., Kobayashi, Y., Carmody, N. C. and Weingold, A. B. (1966). Serial measurements of plasma diamine oxidase (DAO) during normal human pregnancy by an improved method. Amer. J. Obstet. Gynecol. 95, 615-620.
    • (1966) Amer. J. Obstet. Gynecol. , vol.95 , pp. 615-620
    • Southren, A.L.1    Kobayashi, Y.2    Carmody, N.C.3    Weingold, A.B.4
  • 405
    • 0023241014 scopus 로고
    • Effects of dexamethasone on spermidine jV'-acetyltransferase and ornithine decarboxylase activities in rat spleen
    • Stefanelli, C., Flamigni, F., Carati, D., Rossoni, C. and Caldarera, M. (1987). Effects of dexamethasone on spermidine jV'-acetyltransferase and ornithine decarboxylase activities in rat spleen. Biochim. Biophys. Acta 930, 79-86.
    • (1987) Biochim. Biophys. Acta , vol.930 , pp. 79-86
    • Stefanelli, C.1    Flamigni, F.2    Carati, D.3    Rossoni, C.4    Caldarera, M.5
  • 406
    • 0029117707 scopus 로고
    • Identification of topaquinone, as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase
    • Steinebach, V., Groen, B. W., Wijmenga, S. S., Niessen, W. M. A., Jongejan, J. A. and Duine, J. A. (1995). Identification of topaquinone, as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase. Anal. Biochem. 230, 159-166.
    • (1995) Anal. Biochem. , vol.230 , pp. 159-166
    • Steinebach, V.1    Groen, B.W.2    Wijmenga, S.S.3    Niessen, W.M.A.4    Jongejan, J.A.5    Duine, J.A.6
  • 407
    • 0023091144 scopus 로고
    • Polyamines permit the preparation of stable physarum core particles which have a structure similar to those from higher eukaryotes
    • Stone, G. R., Baldwin, J. P. and Carpenter, B. G. (1987). Polyamines permit the preparation of stable Physarum core particles which have a structure similar to those from higher eukaryotes. Biochim. Biophys. Acta 908, 34-45.
    • (1987) Biochim. Biophys. Acta , vol.908 , pp. 34-45
    • Stone, G.R.1    Baldwin, J.P.2    Carpenter, B.G.3
  • 408
    • 0028218441 scopus 로고
    • Comparative enzyme histochemistry of the early and term rat decidua with special attention to decidual regression
    • Straatsburg, I. H. and Gossrau, R. (1994). Comparative enzyme histochemistry of the early and term rat decidua with special attention to decidual regression. Histochem. J. 26, 239-251.
    • (1994) Histochem. J. , vol.26 , pp. 239-251
    • Straatsburg, I.H.1    Gossrau, R.2
  • 409
    • 0021267038 scopus 로고
    • Effects of polyamine depletion on proliferation and differentiation of murine erythroleukemia cells
    • Sugiura, M., Shafman, T. and Kufe, D. (1984). Effects of polyamine depletion on proliferation and differentiation of murine erythroleukemia cells. Cancer Res. 44, 1440-1444.
    • (1984) Cancer Res. , vol.44 , pp. 1440-1444
    • Sugiura, M.1    Shafman, T.2    Kufe, D.3
  • 410
    • 0018398602 scopus 로고
    • Stereochemistry and kinetic isotope effects in the bovine plasma amine oxidase catalysed oxidation of dopamine
    • Summers, M. C., Markovic, R. and Klinman, J. P. (1979). Stereochemistry and kinetic isotope effects in the bovine plasma amine oxidase catalysed oxidation of dopamine. Biochemistry 18, 1969-1979.
    • (1979) Biochemistry , vol.18 , pp. 1969-1979
    • Summers, M.C.1    Markovic, R.2    Klinman, J.P.3
  • 411
    • 0023851255 scopus 로고
    • Induction of ornithine decarboxylase and histidine decarboxylase activities in rat colon mucosa after application of 12-o-tetradecanoylphorbol13-acetate (TPA), sodium deoxycholate and indole
    • Sun, Y. and Li, Y. (1988). Induction of ornithine decarboxylase and histidine decarboxylase activities in rat colon mucosa after application of 12-o-tetradecanoylphorbol13-acetate (TPA), sodium deoxycholate and indole. Cancer Lett. 39, 77-84.
    • (1988) Cancer Lett. , vol.39 , pp. 77-84
    • Sun, Y.1    Li, Y.2
  • 412
    • 0019429488 scopus 로고
    • The relationship between levels and rates of synthesis of polyamines during mammalian cell cycle
    • Sunkara, P. S., Ramakrishna, S., Nishioka, K. and Rao, P. N. (1981). The relationship between levels and rates of synthesis of polyamines during mammalian cell cycle. Life Sciences 28, 1497-1506.
    • (1981) Life Sciences , vol.28 , pp. 1497-1506
    • Sunkara, P.S.1    Ramakrishna, S.2    Nishioka, K.3    Rao, P.N.4
  • 413
    • 0009278626 scopus 로고
    • Some properties of benzylamine oxidase in human aorta
    • Suzuki, O. and Matsumoto, T. (1984). Some properties of benzylamine oxidase in human aorta. Biogenic amines 1, 249-257.
    • (1984) Biogenic Amines , vol.1 , pp. 249-257
    • Suzuki, O.1    Matsumoto, T.2
  • 414
    • 0021630141 scopus 로고
    • Determination of polyamine oxidase activities in human tissues
    • Suzuki, O., Matsumoto, T. and Katsumata, Y. (1984). Determination of polyamine oxidase activities in human tissues. Experientia 40, 838-839.
    • (1984) Experientia , vol.40 , pp. 838-839
    • Suzuki, O.1    Matsumoto, T.2    Katsumata, Y.3
  • 415
    • 0342826362 scopus 로고
    • Oxidation of acetylpolyamines by human diamine oxidase
    • (Eds. Selmeci, L., Brosnan, M. E. and Seiler, N.), Akademiai Kiado, Budapest, Hungary
    • Suzuki, O., Ishikawa, Y. and Matsumoto, T. (1985). Oxidation of acetylpolyamines by human diamine oxidase. In "Recent progress in Polyamine Research" (Eds. Selmeci, L., Brosnan, M. E. and Seiler, N.), pp. 321-327, Akademiai Kiado, Budapest, Hungary.
    • (1985) Recent Progress in Polyamine Research , pp. 321-327
    • Suzuki, O.1    Ishikawa, Y.2    Matsumoto, T.3
  • 416
    • 0001221454 scopus 로고
    • Purification and properties of diamine oxidase from human kidney
    • Suzuki, O. and Matsumoto, T. (1987a). Purification and properties of diamine oxidase from human kidney. Biogenic Amines 4, 237-245.
    • (1987) Biogenic Amines , vol.4 , pp. 237-245
    • Suzuki, O.1    Matsumoto, T.2
  • 417
    • 0342954000 scopus 로고
    • Properties of benzylamine oxidase in human small intestine
    • Suzuki, O. and Matsumoto, T. (1987b). Properties of benzylamine oxidase in human small intestine. Biogenic Amines 4, 45-53.
    • (1987) Biogenic Amines , vol.4 , pp. 45-53
    • Suzuki, O.1    Matsumoto, T.2
  • 418
    • 0019398847 scopus 로고
    • Preparation of amine oxidase from bovine serum by affinity chromatography on aminohexyl-sepharose
    • Svenson, A. and Hynning, P.-Å. (1981). Preparation of amine oxidase from bovine serum by affinity chromatography on aminohexyl-Sepharose. Preparative Biochem. 11, 99-108.
    • (1981) Preparative Biochem. , vol.11 , pp. 99-108
    • Svenson, A.1    Hynning, P.-Å.2
  • 419
    • 0342826361 scopus 로고
    • Histaminase in pregnancy
    • Swanberg, H. (1950). Histaminase in pregnancy. Acta Physiol. Scand. 23, Suppl. 79, 1-69.
    • (1950) Acta Physiol. Scand. , vol.23 , Issue.SUPPL. 79 , pp. 1-69
    • Swanberg, H.1
  • 420
    • 0019142868 scopus 로고
    • Inhibition of lymphocyte growth by spermidine in medium containing fetal bovine serum
    • Swanson, T. L. and Gibbs, G. E. (1980). Inhibition of lymphocyte growth by spermidine in medium containing fetal bovine serum. In Vitro 16, 761-766.
    • (1980) In Vitro , vol.16 , pp. 761-766
    • Swanson, T.L.1    Gibbs, G.E.2
  • 421
    • 0342826360 scopus 로고
    • Untersuchungen über das diaminoxydaseferment (histaminase)
    • Swedin, B. (1943). Untersuchungen über das Diaminoxydaseferment (Histaminase). Acta Med. Scand. 114, 210-215.
    • (1943) Acta Med. Scand. , vol.114 , pp. 210-215
    • Swedin, B.1
  • 422
    • 0009747039 scopus 로고
    • Diamine oxidase
    • Tabor, H. (1951). Diamine oxidase. J. Biol. Chem. 188, 125-136.
    • (1951) J. Biol. Chem. , vol.188 , pp. 125-136
    • Tabor, H.1
  • 423
    • 77049184093 scopus 로고
    • Purification of amine oxidase from beef plasma
    • Tabor, C. W., Tabor, H. and Rosenthal, S. M. (1954). Purification of amine oxidase from beef plasma. J. Biol. Chem. 208, 654-661.
    • (1954) J. Biol. Chem. , vol.208 , pp. 654-661
    • Tabor, C.W.1    Tabor, H.2    Rosenthal, S.M.3
  • 424
    • 76549155767 scopus 로고
    • Spermidine, spermine and related amines
    • Tabor, H. and Tabor, C. W. (1964). Spermidine, spermine and related amines. Pharmacol. Rev. 16, 245-300.
    • (1964) Pharmacol. Rev. , vol.16 , pp. 245-300
    • Tabor, H.1    Tabor, C.W.2
  • 425
    • 0000590881 scopus 로고
    • Identification of the aminoaldehydes produced by the oxidation of spermine and spermidine with purified plasma amine oxidase
    • Tabor, C. W., Tabor, H. and Bachrach, U. (1964a). Identification of the aminoaldehydes produced by the oxidation of spermine and spermidine with purified plasma amine oxidase. J. Biol. Chem. 239, 2194-2203.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2194-2203
    • Tabor, C.W.1    Tabor, H.2    Bachrach, U.3
  • 426
    • 0343696854 scopus 로고
    • Further studies on the aminoaldehydes formed by the enzymatic oxidation of spermine and spermidine
    • Tabor, C. W., Tabor, H., McEwen, Jr. C. M. and Kellogg, P. D. (1964b). Further studies on the aminoaldehydes formed by the enzymatic oxidation of spermine and spermidine. Fed. Proc. 23, 385.
    • (1964) Fed. Proc. , vol.23 , pp. 385
    • Tabor, C.W.1    Tabor, H.2    McEwen C.M., Jr.3    Kellogg, P.D.4
  • 427
    • 0017102423 scopus 로고
    • 1,4-Diaminobutane (Putrescine), spermidine and spermine
    • Tabor, C. W. and Tabor, H. (1976). 1,4-Diaminobutane (Putrescine), spermidine and spermine. Ann. Rev. Biochem. 45, 285-306.
    • (1976) Ann. Rev. Biochem. , vol.45 , pp. 285-306
    • Tabor, C.W.1    Tabor, H.2
  • 429
    • 84998213749 scopus 로고
    • Localization of diamine oxidase and D-amino acid oxidase in kidney, demonstrated by means of immunohistochemical method
    • Takano, K., Suzuki, T. and Yasuda, K. (1970). Localization of diamine oxidase and D-amino acid oxidase in kidney, demonstrated by means of immunohistochemical method. Acta Histochem. Cytochem. 3, 105-113.
    • (1970) Acta Histochem. Cytochem. , vol.3 , pp. 105-113
    • Takano, K.1    Suzuki, T.2    Yasuda, K.3
  • 430
    • 0029584729 scopus 로고
    • Transcriptional regulation of genes for ornithine cycle enzymes
    • Takiguchi, M. and Mori, M. (1995). Transcriptional regulation of genes for ornithine cycle enzymes. Biochem. J. 312, 649-659.
    • (1995) Biochem. J. , vol.312 , pp. 649-659
    • Takiguchi, M.1    Mori, M.2
  • 431
    • 0029131460 scopus 로고
    • Point mutation of ornithine decarboxylase gene in human hepatocellular carcinoma
    • Tamori, A., Nishiguchi, S., Kuroki, T., Koh, N., Kobayashi, K., Yano, Y. and Otani, S. (1995). Point mutation of ornithine decarboxylase gene in human hepatocellular carcinoma. Cancer Res. 55, 3500-3503.
    • (1995) Cancer Res. , vol.55 , pp. 3500-3503
    • Tamori, A.1    Nishiguchi, S.2    Kuroki, T.3    Koh, N.4    Kobayashi, K.5    Yano, Y.6    Otani, S.7
  • 432
    • 0024538484 scopus 로고
    • Kinetic studies on the inhibition mechanism of diamine oxidase from porcine kidney by aminoguani-dine
    • Tamura, H., Horiike, K., Fukuda, H. and Watanabe, T. (1989). Kinetic studies on the inhibition mechanism of diamine oxidase from porcine kidney by aminoguani-dine. J. Biochem. 105, 299-306.
    • (1989) J. Biochem. , vol.105 , pp. 299-306
    • Tamura, H.1    Horiike, K.2    Fukuda, H.3    Watanabe, T.4
  • 433
    • 0022612877 scopus 로고
    • Enzymology of monoamine oxidase
    • Tipton, K. F. (1986). Enzymology of monoamine oxidase. Cell Biochem. Function 4, 79-87.
    • (1986) Cell Biochem. Function , vol.4 , pp. 79-87
    • Tipton, K.F.1
  • 434
    • 0028294581 scopus 로고
    • Regulation of putrescine export in lipopolysaccharide or IFN-γ-activated murine monocytic-leukemic RAW 264 cells
    • Tjandrawinata, R. R., Hawel III, L. and Byus, C. V. (1994). Regulation of putrescine export in lipopolysaccharide or IFN-γ-activated murine monocytic-leukemic RAW 264 cells. J. Immunol. 152, 3039-3052.
    • (1994) J. Immunol. , vol.152 , pp. 3039-3052
    • Tjandrawinata, R.R.1    Hawel L. III2    Byus, C.V.3
  • 435
    • 0028797750 scopus 로고
    • Regulation of the efflux of putrescine and cadaverine from rapidly growing cultured RAW 2264 cells by extracellular putrescine
    • Tjandrawinata, R. R. and Byus, C. V. (1995). Regulation of the efflux of putrescine and cadaverine from rapidly growing cultured RAW 2264 cells by extracellular putrescine. Biochem. J. 305, 291-299.
    • (1995) Biochem. J. , vol.305 , pp. 291-299
    • Tjandrawinata, R.R.1    Byus, C.V.2
  • 436
    • 0028800002 scopus 로고
    • Exposure to ornithine results in excessive accumulation of putrescine and apoptotic cell death in ornithine decarboxylase overproducing mouse myeloma cells
    • Tobias, K. E. and Kahana, C. (1995). Exposure to ornithine results in excessive accumulation of putrescine and apoptotic cell death in ornithine decarboxylase overproducing mouse myeloma cells. Cell Growth and Differentiation 6, 1279-1285.
    • (1995) Cell Growth and Differentiation , vol.6 , pp. 1279-1285
    • Tobias, K.E.1    Kahana, C.2
  • 437
    • 0031469938 scopus 로고    scopus 로고
    • Excess putrescine accumulation inhibits the formation of modified eucaryotic initiation factor 5A (elF-5A) and induces apoptosis
    • Tome, M. E., Fiser, S. M., Payne, C. M. and Gerner, E. W. (1997). Excess putrescine accumulation inhibits the formation of modified eucaryotic initiation factor 5A (elF-5A) and induces apoptosis. Biochem. J. 328, 847-854.
    • (1997) Biochem. J. , vol.328 , pp. 847-854
    • Tome, M.E.1    Fiser, S.M.2    Payne, C.M.3    Gerner, E.W.4
  • 439
    • 0014369731 scopus 로고
    • Determination of plasma diamine oxidase (histaminase) in clinical practise
    • Tryding, N. and Willert, B. (1968). Determination of plasma diamine oxidase (histaminase) in clinical practise. Scand. J. Clin. Lab. Invest. 22, 29-32.
    • (1968) Scand. J. Clin. Lab. Invest. , vol.22 , pp. 29-32
    • Tryding, N.1    Willert, B.2
  • 440
    • 0023946253 scopus 로고
    • Purification by affinity chromatography and characterization of porcine liver cytoplasmic polyamine oxidase
    • Tsukada, T., Furusaka, S., Maekawa, S., Hibasami, H. and Nakashima, K. (1988). Purification by affinity chromatography and characterization of porcine liver cytoplasmic polyamine oxidase. Int. J. Biochem. 20, 695-702.
    • (1988) Int. J. Biochem. , vol.20 , pp. 695-702
    • Tsukada, T.1    Furusaka, S.2    Maekawa, S.3    Hibasami, H.4    Nakashima, K.5
  • 441
    • 0018191565 scopus 로고
    • Purification and properties of human amniotic fluid diamine oxidase
    • Tufvesson, G. (1978a). Purification and properties of human amniotic fluid diamine oxidase. Scand. J. Clin. Lab. Invest. 38, 463-472.
    • (1978) Scand. J. Clin. Lab. Invest. , vol.38 , pp. 463-472
    • Tufvesson, G.1
  • 442
    • 0018141999 scopus 로고
    • A comparison between diamine oxidases from human post-heparin blood serum, pregnancy blood serum and amniotic fluid
    • Tufvesson, G. (1978b). A comparison between diamine oxidases from human post-heparin blood serum, pregnancy blood serum and amniotic fluid. Scand. J. Clin. Lab. Invest. 38, 473-476.
    • (1978) Scand. J. Clin. Lab. Invest. , vol.38 , pp. 473-476
    • Tufvesson, G.1
  • 444
    • 0343696853 scopus 로고
    • Studies on polyamines II. Metabolism of spermidine and spermine by amine oxidase in beef serum
    • Unemoto, T. (1963). Studies on polyamines II. Metabolism of spermidine and spermine by amine oxidase in beef serum. Chem. Pharm. Bull. 11, 1255-1264.
    • (1963) Chem. Pharm. Bull. , vol.11 , pp. 1255-1264
    • Unemoto, T.1
  • 445
    • 0342391633 scopus 로고
    • Purification and properties of histaminase from hog kidney
    • Uozumi, K., Nakahara, I., Higashi, T. and Sakamoto, Y. (1964). Purification and properties of histaminase from hog kidney. J. Biochem. 56, 601-603.
    • (1964) J. Biochem. , vol.56 , pp. 601-603
    • Uozumi, K.1    Nakahara, I.2    Higashi, T.3    Sakamoto, Y.4
  • 446
    • 0019479340 scopus 로고
    • Uptake and excretion of polyamines from baby hamster kidney cells (BHK-21/cl3). The effect of serum on confluent cell cultures
    • Wallace, H. M. and Keir, H. M. (1981). Uptake and excretion of polyamines from baby hamster kidney cells (BHK-21/cl3). The effect of serum on confluent cell cultures. Biochim. Biophys. Acta 676, 25-30.
    • (1981) Biochim. Biophys. Acta , vol.676 , pp. 25-30
    • Wallace, H.M.1    Keir, H.M.2
  • 447
    • 0343261188 scopus 로고
    • Polyamine acetylation and excretion by mammalian cells in culture
    • (Eds., Selmeci, L., Brosnan, M. E. and Seiler, N.), Akademiai Kiado, Budapest, Hungary
    • Wallace, H. M. and Keir, H. M. (1985). Polyamine acetylation and excretion by mammalian cells in culture. In "Recent progress in polyamine research" (Eds., Selmeci, L., Brosnan, M. E. and Seiler, N.), pp. 297-304, Akademiai Kiado, Budapest, Hungary.
    • (1985) Recent Progress in Polyamine Research , pp. 297-304
    • Wallace, H.M.1    Keir, H.M.2
  • 449
    • 0023633270 scopus 로고
    • Polyamine catabolism in mammalian cells: Excretion and acetylation
    • Wallace, H. M. (1987). Polyamine catabolism in mammalian cells: excretion and acetylation. Med. Sci. Res. 15, 1437-1440.
    • (1987) Med. Sci. Res. , vol.15 , pp. 1437-1440
    • Wallace, H.M.1
  • 450
    • 0023692753 scopus 로고
    • Acetylation of spermidine and methylglyoxal bis(guanylhydrazone) in baby-hamster kidney cells (BHK-21/C13)
    • Wallace, H. M., Nuttall, M. E. and Robinson, F. C. (1988). Acetylation of spermidine and methylglyoxal bis(guanylhydrazone) in baby-hamster kidney cells (BHK-21/C13). Biochem. J. 253, 223-227.
    • (1988) Biochem. J. , vol.253 , pp. 223-227
    • Wallace, H.M.1    Nuttall, M.E.2    Robinson, F.C.3
  • 451
    • 0028533755 scopus 로고
    • Joint chromatographic purification of bovine serum ceruloplasmin and amine oxidase
    • Wang, X. T., Dumoulin, M. J., Befani, O., Mondovi, B. and Mateescu, M. A, (1994). Joint chromatographic purification of bovine serum ceruloplasmin and amine oxidase. Preparative Biochem. 24, 237-250.
    • (1994) Preparative Biochem. , vol.24 , pp. 237-250
    • Wang, X.T.1    Dumoulin, M.J.2    Befani, O.3    Mondovi, B.4    Mateescu, M.A.5
  • 453
    • 0014962761 scopus 로고
    • Carbohydrate content of bovine plasma amine oxidase and isolation of a carbohydrate-containing fragment attached to asparagine
    • Watanabe, K. and Yasunobu, K. T. (1970). Carbohydrate content of bovine plasma amine oxidase and isolation of a carbohydrate-containing fragment attached to asparagine. J. Biol. Chem. 245, 4612-4617.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4612-4617
    • Watanabe, K.1    Yasunobu, K.T.2
  • 454
    • 0018888890 scopus 로고
    • Spermine oxidation products are selectively toxic to fibroblasts in cultures of normal human prostatic epithelium
    • Webber, M. M. and Chaproniere-Rickenberg, D. (1980). Spermine oxidation products are selectively toxic to fibroblasts in cultures of normal human prostatic epithelium. Cell Biol. Int. Rep. 4, 185-193.
    • (1980) Cell Biol. Int. Rep. , vol.4 , pp. 185-193
    • Webber, M.M.1    Chaproniere-Rickenberg, D.2
  • 455
    • 0018138313 scopus 로고
    • Immunohistochemical localisation of histaminase (diamine oxidase) in decidual cells of human placenta
    • Weisburger, W. R., Mendelsohn, G., Eggleston, J. C. and Baylin, S. B. (1978). Immunohistochemical localisation of histaminase (diamine oxidase) in decidual cells of human placenta. Lab. Invest. 38, 703-706.
    • (1978) Lab. Invest. , vol.38 , pp. 703-706
    • Weisburger, W.R.1    Mendelsohn, G.2    Eggleston, J.C.3    Baylin, S.B.4
  • 456
    • 0342826355 scopus 로고
    • Über die histaminzerstörende fähigkeit des schwangerenblutes
    • Werle, E. and Effkemann, G. (1940). Über die histaminzerstörende Fähigkeit des Schwangerenblutes. Arch. Gynaek. 170, 82-89.
    • (1940) Arch. Gynaek. , vol.170 , pp. 82-89
    • Werle, E.1    Effkemann, G.2
  • 457
    • 0342391630 scopus 로고
    • Zur oxydativen desaminierung von spermin und spermidin durch rinderplasma
    • Werle, E. and Roewer, F. (1954). Zur oxydativen Desaminierung von Spermin und Spermidin durch Rinderplasma. Biochem. Zeitschr. 325, 550-554.
    • (1954) Biochem. Zeitschr. , vol.325 , pp. 550-554
    • Werle, E.1    Roewer, F.2
  • 458
    • 0000466665 scopus 로고
    • Histamine
    • (Eds. Gallin, J. I., Goldstein, I. M. and Snyderman, R.), Raven Press, New York, USA
    • White, M.W. and Kaliner, M. A. (1988). Histamine. In "Inflammation: Basic principles and clinical correlates" (Eds. Gallin, J. I., Goldstein, I. M. and Snyderman, R.), pp. 169-187, Raven Press, New York, USA.
    • (1988) Inflammation: Basic Principles and Clinical Correlates , pp. 169-187
    • White, M.W.1    Kaliner, M.A.2
  • 459
    • 0019201214 scopus 로고
    • Subcellular location of semicarbazide-sensitive amine oxidase in rat aorta
    • Wibo, M., Duong, A. T. and Godfraind, T. (1980). Subcellular location of semicarbazide-sensitive amine oxidase in rat aorta. Eur. J. Biochem. 112, 87-94.
    • (1980) Eur. J. Biochem. , vol.112 , pp. 87-94
    • Wibo, M.1    Duong, A.T.2    Godfraind, T.3
  • 460
    • 0028319789 scopus 로고
    • Diamine oxidase: An overview of historical, biochemical and functional aspects
    • Wolvekamp, M. C. J. and de Bruin, R. W. F. (1994). Diamine oxidase: an overview of historical, biochemical and functional aspects. Dig. Dis. 12, 2-14.
    • (1994) Dig. Dis. , vol.12 , pp. 2-14
    • Wolvekamp, M.C.J.1    De Bruin, R.W.F.2
  • 461
    • 0001750845 scopus 로고
    • Monoamine oxidase. II. Copper, one of the prosthetic groups of plasma monoamine oxidase
    • Yamada, H. and Yasunobu, K. T. (1962a). Monoamine oxidase. II. Copper, one of the prosthetic groups of plasma monoamine oxidase. J. Biol. Chem. 237, 3077-3082.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3077-3082
    • Yamada, H.1    Yasunobu, K.T.2
  • 462
    • 0001750844 scopus 로고
    • Monoamine oxidase. I. Purification, crystallisation and properties of plasma monoamine oxidase
    • Yamada, H. and Yasunobu, K. T. (1962b). Monoamine oxidase. I. Purification, crystallisation and properties of plasma monoamine oxidase. J. Biol. Chem. 237, 1511-1516.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1511-1516
    • Yamada, H.1    Yasunobu, K.T.2
  • 463
  • 465
    • 0017187001 scopus 로고
    • The molecular, mechanistic and immunological properties of amine oxidases
    • Yasunobu, K. T., Ishizaki, H. and Minamiura, N. (1976). The molecular, mechanistic and immunological properties of amine oxidases. Mol. Cell. Biochem. 13, 3-29.
    • (1976) Mol. Cell. Biochem. , vol.13 , pp. 3-29
    • Yasunobu, K.T.1    Ishizaki, H.2    Minamiura, N.3
  • 466
    • 0025667309 scopus 로고
    • Oxidative deamination of aliphatic amines by rat aorta semicarbazide-sensitive amine oxidase
    • Yu, P. H. (1990). Oxidative deamination of aliphatic amines by rat aorta semicarbazide-sensitive amine oxidase. J. Pharm. Pharmacol. 42, 882-884.
    • (1990) J. Pharm. Pharmacol. , vol.42 , pp. 882-884
    • Yu, P.H.1
  • 467
    • 0028314764 scopus 로고
    • Characterization of human serum and umbilical artery semicarbazide-sensitive amine oxidase
    • Yu, P. H., Zuo, D.-M. and Davis, B. A. (1994). Characterization of human serum and umbilical artery semicarbazide-sensitive amine oxidase. Biochem. Pharmacol. 47, 1055-1059.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 1055-1059
    • Yu, P.H.1    Zuo, D.-M.2    Davis, B.A.3
  • 468
    • 0017167095 scopus 로고
    • Histaminase release from human granulocytes
    • Zeiger, R. S., Twarog, F. J. and Colten, H. R. (1976a). Histaminase release from human granulocytes. J. Exp. Med. 144, 1049-1061.
    • (1976) J. Exp. Med. , vol.144 , pp. 1049-1061
    • Zeiger, R.S.1    Twarog, F.J.2    Colten, H.R.3
  • 470
    • 84982334045 scopus 로고
    • Über den enzymatischen abbau von histamin und diaminen
    • Zeller, E. A. (1938a). Über den enzymatischen Abbau von Histamin und Diaminen. Helv. Chim. Acta 21, 880-890.
    • (1938) Helv. Chim. Acta , vol.21 , pp. 880-890
    • Zeller, E.A.1
  • 471
    • 84982064210 scopus 로고
    • Zur kenntnis der diamin-oxydase
    • Zeller, E. A. (1938b). Zur Kenntnis der Diamin-oxydase. Helv. Chim. Acta 21, 1645-1665.
    • (1938) Helv. Chim. Acta , vol.21 , pp. 1645-1665
    • Zeller, E.A.1
  • 472
    • 0342826354 scopus 로고
    • Ueber eine einfache farbreaktion als schwangerschaftsnachweis
    • Zeller, E. A. (1941). Ueber eine einfache Farbreaktion als Schwangerschaftsnachweis. Schw. Med. Wchsch. 71, 1349-1351.
    • (1941) Schw. Med. Wchsch. , vol.71 , pp. 1349-1351
    • Zeller, E.A.1
  • 473
    • 0009469439 scopus 로고
    • Diamine oxidases
    • Zeller, E. A. (1963). Diamine oxidases. The Enzymes 8, 313-335.
    • (1963) The Enzymes , vol.8 , pp. 313-335
    • Zeller, E.A.1
  • 474
    • 0029094181 scopus 로고
    • CDNA sequences of variant forms of human placenta diamine oxidase
    • Zhang, X., Kim, J. and McIntire, W. S. (1995). cDNA sequences of variant forms of human placenta diamine oxidase. Biochemical genetics 33, 261-268.
    • (1995) Biochemical Genetics , vol.33 , pp. 261-268
    • Zhang, X.1    Kim, J.2    McIntire, W.S.3
  • 475
    • 0030583734 scopus 로고    scopus 로고
    • Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta
    • Zhang, X. and McIntire, W. S. (1996). Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta. Gene 179, 279-286.
    • (1996) Gene , vol.179 , pp. 279-286
    • Zhang, X.1    McIntire, W.S.2
  • 476
    • 0028366164 scopus 로고
    • Semicarbazide-sensitive amine oxidase and monoamine oxidase in rat brain microvessels, meninges, retina and eye sclera
    • Zuo, D.-M. and Yu, P. H. (1994). Semicarbazide-sensitive amine oxidase and monoamine oxidase in rat brain microvessels, meninges, retina and eye sclera. Brain Res. Bull. 33, 307-311.
    • (1994) Brain Res. Bull. , vol.33 , pp. 307-311
    • Zuo, D.-M.1    Yu, P.H.2


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