메뉴 건너뛰기




Volumn 49, Issue 2, 2011, Pages 171-176

Effects of amines and aminoalcohols on bovine intestine alkaline phosphatase activity

Author keywords

Alkaline phosphatase; Amine; Aminoalcohol; Bovine intestine alkaline phosphatase; Enzyme immunoassay

Indexed keywords

ALKALINE PHOSPHATASE; ALKALINE PHOSPHATASE ACTIVITY; AMINO ALCOHOLS; DIETHANOLAMINE; DIMETHYLAMINES; ENZYME IMMUNOASSAY; ETHANOLAMINES; ETHYLAMINE; P-NITROPHENYL PHOSPHATE; SENSITIVE ASSAY; TRIETHANOLAMINES;

EID: 79959893508     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2011.04.019     Document Type: Article
Times cited : (16)

References (37)
  • 1
    • 77956917564 scopus 로고
    • E. coli alkaline phosphatase
    • Academic Press, New York
    • Reid T.W., Wilson I.B. E. coli alkaline phosphatase. The enzymes 1971, vol. 4:373-415. Academic Press, New York. 3rd ed.
    • (1971) The enzymes , vol.4 , pp. 373-415
    • Reid, T.W.1    Wilson, I.B.2
  • 2
    • 77956925467 scopus 로고
    • Mammalian alkaline phosphatases
    • Academic Press, New York
    • Fernley H.N. Mammalian alkaline phosphatases. The enzymes 1971, vol. 4:417-447. Academic Press, New York. 3rd ed.
    • (1971) The enzymes , vol.4 , pp. 417-447
    • Fernley, H.N.1
  • 3
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures
    • Kim E.E., Wyckoff H.W. Reaction mechanism of alkaline phosphatase based on crystal structures. J Mol Biol 1991, 218:449-464.
    • (1991) J Mol Biol , vol.218 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 4
    • 18944395290 scopus 로고    scopus 로고
    • Characterization of structural and catalytic differences in rat intestinal alkaline phosphatase isozymes
    • Harada T., Koyama I., Matsunaga T., Kikuno A., Kasahara T., Hassimoto M., et al. Characterization of structural and catalytic differences in rat intestinal alkaline phosphatase isozymes. FEBS J 2005, 272:2477-2486.
    • (2005) FEBS J , vol.272 , pp. 2477-2486
    • Harada, T.1    Koyama, I.2    Matsunaga, T.3    Kikuno, A.4    Kasahara, T.5    Hassimoto, M.6
  • 5
    • 0034705337 scopus 로고    scopus 로고
    • A revised mechanism for the alkaline phosphatase reaction involving three metal ions
    • Stec B., Holtz K.M., Kantrowitz E.R. A revised mechanism for the alkaline phosphatase reaction involving three metal ions. J Mol Biol 2000, 299:1303-1311.
    • (2000) J Mol Biol , vol.299 , pp. 1303-1311
    • Stec, B.1    Holtz, K.M.2    Kantrowitz, E.R.3
  • 6
    • 16644387077 scopus 로고    scopus 로고
    • Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase
    • de Backer M.M.E., McSweeney S., Lindley P.F., Hough E. Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase. Acta Cryst 2004, D60:1555-1561.
    • (2004) Acta Cryst , vol.60 , pp. 1555-1561
    • de Backer, M.M.E.1    McSweeney, S.2    Lindley, P.F.3    Hough, E.4
  • 7
    • 0021098998 scopus 로고
    • 31P nuclear magnetic resonance of phosphoenzyme intermediates of alkaline phosphatase
    • Gettins P., Coleman J.E. 31P nuclear magnetic resonance of phosphoenzyme intermediates of alkaline phosphatase. J Biol Chem 1983, 258:408-416.
    • (1983) J Biol Chem , vol.258 , pp. 408-416
    • Gettins, P.1    Coleman, J.E.2
  • 8
    • 0028845411 scopus 로고
    • Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatase
    • Murphy J.E., Tibbitts T.T., Kantrowitz E.R. Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatase. J Mol Biol 1995, 253:604-617.
    • (1995) J Mol Biol , vol.253 , pp. 604-617
    • Murphy, J.E.1    Tibbitts, T.T.2    Kantrowitz, E.R.3
  • 9
    • 0021321955 scopus 로고
    • A rapid, sensitive methods for detection of alkaline phosphatase-conjugated anti-antibody on Western blots
    • Blake M.S., Johnston K.H., Russell-Jones G.R., Gotschlich E.C. A rapid, sensitive methods for detection of alkaline phosphatase-conjugated anti-antibody on Western blots. Anal Biochem 1984, 136:175-179.
    • (1984) Anal Biochem , vol.136 , pp. 175-179
    • Blake, M.S.1    Johnston, K.H.2    Russell-Jones, G.R.3    Gotschlich, E.C.4
  • 10
    • 0023046909 scopus 로고
    • Preparation of oligodeoxynucleotide-alkaline phosphatase conjugated and their use as hybridization probes
    • Jablonski E., Moomaw E.W., Tullis R.H., Ruth J.L. Preparation of oligodeoxynucleotide-alkaline phosphatase conjugated and their use as hybridization probes. Nucleic Acids Res 1986, 14:6115-6128.
    • (1986) Nucleic Acids Res , vol.14 , pp. 6115-6128
    • Jablonski, E.1    Moomaw, E.W.2    Tullis, R.H.3    Ruth, J.L.4
  • 11
    • 0001677766 scopus 로고    scopus 로고
    • Automation of immunoassays
    • Academic Press, New York, E.P. Diamandis, T.K. Christopoulos (Eds.)
    • Chan D.W. Automation of immunoassays. Immunoassay 1996, 483-504. Academic Press, New York. E.P. Diamandis, T.K. Christopoulos (Eds.).
    • (1996) Immunoassay , pp. 483-504
    • Chan, D.W.1
  • 12
    • 3142578763 scopus 로고    scopus 로고
    • Academic Press, New York, E.P. Diamandis, T.K. Christopoulos (Eds.)
    • Gosling J.P. Immunoassay 1996, 287-308. Academic Press, New York. E.P. Diamandis, T.K. Christopoulos (Eds.).
    • (1996) Immunoassay , pp. 287-308
    • Gosling, J.P.1
  • 13
    • 0026570064 scopus 로고
    • Single-step purification of F(ab′)2 fragments of mouse monoclonal antibodies (immunoglobulins G1) by hydrophobic interaction high performance liquid chromatography using TSKgel Phenyl-5PW
    • Morimoto K., Inouye K. Single-step purification of F(ab′)2 fragments of mouse monoclonal antibodies (immunoglobulins G1) by hydrophobic interaction high performance liquid chromatography using TSKgel Phenyl-5PW. J Biochem Biophys Methods 1992, 24:107-117.
    • (1992) J Biochem Biophys Methods , vol.24 , pp. 107-117
    • Morimoto, K.1    Inouye, K.2
  • 14
    • 0027462914 scopus 로고
    • Single-step purification of F(ab′)2μ fragments of mouse monoclonal antibodies (immunoglobulins M) by hydrophobic interaction high-performance liquid chromatography using TSKgel ether-5PW
    • Morimoto K., Inouye K. Single-step purification of F(ab′)2μ fragments of mouse monoclonal antibodies (immunoglobulins M) by hydrophobic interaction high-performance liquid chromatography using TSKgel ether-5PW. J Biochem Biophys Methods 1993, 26:27-39.
    • (1993) J Biochem Biophys Methods , vol.26 , pp. 27-39
    • Morimoto, K.1    Inouye, K.2
  • 15
    • 0030837906 scopus 로고    scopus 로고
    • A sensitive enzyme immunoassay of human thyroid-stimulating hormone (TSH) using bispecific F(ab′)2 fragments recognizing polymerized alkaline phosphatase and TSH
    • Morimoto K., Inouye K. A sensitive enzyme immunoassay of human thyroid-stimulating hormone (TSH) using bispecific F(ab′)2 fragments recognizing polymerized alkaline phosphatase and TSH. J Immunol Methods 1997, 205:81-90.
    • (1997) J Immunol Methods , vol.205 , pp. 81-90
    • Morimoto, K.1    Inouye, K.2
  • 16
    • 0033025678 scopus 로고    scopus 로고
    • Method for the preparation of bispecific F(ab′)2μ fragments from mouse monoclonal antibodies of the immunoglobulin M class and characterization of the fragments
    • Morimoto K., Inouye K. Method for the preparation of bispecific F(ab′)2μ fragments from mouse monoclonal antibodies of the immunoglobulin M class and characterization of the fragments. J Immunol Methods 1999, 224:43-50.
    • (1999) J Immunol Methods , vol.224 , pp. 43-50
    • Morimoto, K.1    Inouye, K.2
  • 17
    • 0019286674 scopus 로고
    • Buffer-induced activation of calf intestinal alkaline phosphate
    • Bannister A., Foster R.L. Buffer-induced activation of calf intestinal alkaline phosphate. Eur J Biochem 1980, 113:199-203.
    • (1980) Eur J Biochem , vol.113 , pp. 199-203
    • Bannister, A.1    Foster, R.L.2
  • 18
    • 0027360773 scopus 로고
    • Kinetic parameters for the cleaved substrate, and enzyme and substrate stability, vary with the phosphoacceptor in alkaline phosphatase catalysis
    • Stinson R.A. Kinetic parameters for the cleaved substrate, and enzyme and substrate stability, vary with the phosphoacceptor in alkaline phosphatase catalysis. Clin Chem 1993, 39:2293-2297.
    • (1993) Clin Chem , vol.39 , pp. 2293-2297
    • Stinson, R.A.1
  • 19
    • 0032483442 scopus 로고    scopus 로고
    • Genetic complexity, structure, and characterization of highly active bovine intestinal alkaline phosphatases
    • Manes T., Hoylaerts M.F., Muller R., Lottspeich F., Holke W., Millan J.L. Genetic complexity, structure, and characterization of highly active bovine intestinal alkaline phosphatases. J Biol Chem 1998, 273:23353-23360.
    • (1998) J Biol Chem , vol.273 , pp. 23353-23360
    • Manes, T.1    Hoylaerts, M.F.2    Muller, R.3    Lottspeich, F.4    Holke, W.5    Millan, J.L.6
  • 20
    • 0023259042 scopus 로고
    • Phosphotransferase activity of human alkaline phosphatase and the role of enzyme Zn2+
    • Stinson R.A., McPhee J.L., Collier H.B. Phosphotransferase activity of human alkaline phosphatase and the role of enzyme Zn2+. Biochim Biophys Acta 1987, 913:272-278.
    • (1987) Biochim Biophys Acta , vol.913 , pp. 272-278
    • Stinson, R.A.1    McPhee, J.L.2    Collier, H.B.3
  • 21
    • 76849102308 scopus 로고    scopus 로고
    • Hofmeister effects on activity and stability of alkaline phosphatase
    • Yang Z., Liu X.J., Chen C., Halling P.J. Hofmeister effects on activity and stability of alkaline phosphatase. Biochim Biophys Acta 2010, 1084:821-828.
    • (2010) Biochim Biophys Acta , vol.1084 , pp. 821-828
    • Yang, Z.1    Liu, X.J.2    Chen, C.3    Halling, P.J.4
  • 22
    • 0026799337 scopus 로고
    • Effects of salts on thermolysin: activation of hydrolysis and synthesis of N-carbobenzoxy-l-aspartyl-l-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin
    • Inouye K. Effects of salts on thermolysin: activation of hydrolysis and synthesis of N-carbobenzoxy-l-aspartyl-l-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin. J Biochem 1992, 112:335-340.
    • (1992) J Biochem , vol.112 , pp. 335-340
    • Inouye, K.1
  • 23
    • 0029863639 scopus 로고    scopus 로고
    • Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts
    • Inouye K., Lee S.-B., Tonomura B. Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts. Biochem J 1996, 315:133-138.
    • (1996) Biochem J , vol.315 , pp. 133-138
    • Inouye, K.1    Lee, S.-B.2    Tonomura, B.3
  • 24
    • 0031979332 scopus 로고    scopus 로고
    • Effect of salts on the solubility of thermolysin: a remarkable increase in the solubility as well as the activity by the addition of salts without aggregation or dispersion of thermolysin
    • Inouye K., Kuzuya K., Tonomura B. Effect of salts on the solubility of thermolysin: a remarkable increase in the solubility as well as the activity by the addition of salts without aggregation or dispersion of thermolysin. J Biochem 1998, 123:847-852.
    • (1998) J Biochem , vol.123 , pp. 847-852
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 25
    • 56949087215 scopus 로고    scopus 로고
    • Comparative enzymology in the alkaline phosphates superfamily to determine the catalytic role of an active-site metal ion
    • Zalatan J.G., Fenn T.D., Herschlag D. Comparative enzymology in the alkaline phosphates superfamily to determine the catalytic role of an active-site metal ion. J Mol Biol 2008, 384:1174-1189.
    • (2008) J Mol Biol , vol.384 , pp. 1174-1189
    • Zalatan, J.G.1    Fenn, T.D.2    Herschlag, D.3
  • 26
    • 0000074647 scopus 로고    scopus 로고
    • Academic Press, New York, E.P. Diamandis, T.K. Christopoulos (Eds.)
    • Christopoulos T.K., Diamandis E.P. Immunoassay 1996, 309-335. Academic Press, New York. E.P. Diamandis, T.K. Christopoulos (Eds.).
    • (1996) Immunoassay , pp. 309-335
    • Christopoulos, T.K.1    Diamandis, E.P.2
  • 27
    • 0003011733 scopus 로고    scopus 로고
    • Academic Press, New York, E.P. Diamandis, T.K. Christopoulos (Eds.)
    • Kricka L.J. Immunoassay 1996, 337-353. Academic Press, New York. E.P. Diamandis, T.K. Christopoulos (Eds.).
    • (1996) Immunoassay , pp. 337-353
    • Kricka, L.J.1
  • 28
    • 79955794958 scopus 로고    scopus 로고
    • Study on chemiluminescent enzyme immunoassay for the measurement of leptin
    • Sekiguchi S., Kohno H., Yasukawa K., Inouye K. Study on chemiluminescent enzyme immunoassay for the measurement of leptin. Biosci Biotechnol Biochem 2011, 75:752-756.
    • (2011) Biosci Biotechnol Biochem , vol.75 , pp. 752-756
    • Sekiguchi, S.1    Kohno, H.2    Yasukawa, K.3    Inouye, K.4
  • 29
    • 77049240611 scopus 로고
    • Some properties of alkaline phosphatase of cow's milk and calf intestinal mucosa
    • Morton R.K. Some properties of alkaline phosphatase of cow's milk and calf intestinal mucosa. Biochem J 1955, 60:573-582.
    • (1955) Biochem J , vol.60 , pp. 573-582
    • Morton, R.K.1
  • 30
    • 0016151185 scopus 로고
    • Intestinal alkaline phosphatase. Catalytic properties and half of the sites reactivity
    • Chappelet-Tordo D., Fosset M., Iwatsubo M., Gache C., Lazdunski M. Intestinal alkaline phosphatase. Catalytic properties and half of the sites reactivity. Biochemistry 1974, 13:1788-1795.
    • (1974) Biochemistry , vol.13 , pp. 1788-1795
    • Chappelet-Tordo, D.1    Fosset, M.2    Iwatsubo, M.3    Gache, C.4    Lazdunski, M.5
  • 31
    • 0002782180 scopus 로고
    • Kinetic behaviour of calf-intestinal alkaline phosphatase with 4-methylumbelliferyl phosphate
    • Fernley H.N., Waker P.G. Kinetic behaviour of calf-intestinal alkaline phosphatase with 4-methylumbelliferyl phosphate. Biochem J 1965, 97:95-103.
    • (1965) Biochem J , vol.97 , pp. 95-103
    • Fernley, H.N.1    Waker, P.G.2
  • 32
    • 0000457907 scopus 로고
    • Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents
    • Plocke D.J., Vallee B.L. Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents. Biochemistry 1962, 1:1039-1043.
    • (1962) Biochemistry , vol.1 , pp. 1039-1043
    • Plocke, D.J.1    Vallee, B.L.2
  • 33
    • 0014940473 scopus 로고
    • Phosphate binding to alkaline phosphatase. Metal ion dependence
    • Applebury M.L., Johnson B.P., Coleman J.E. Phosphate binding to alkaline phosphatase. Metal ion dependence. J Biol Chem 1970, 245:4968-4976.
    • (1970) J Biol Chem , vol.245 , pp. 4968-4976
    • Applebury, M.L.1    Johnson, B.P.2    Coleman, J.E.3
  • 34
    • 0042385015 scopus 로고    scopus 로고
    • Effect of extraneous zinc on calf intestinal alkaline phosphatase
    • Yan S., Liu L., Tian X., Zhang Y., Zhou H. Effect of extraneous zinc on calf intestinal alkaline phosphatase. J Protein Chem 2003, 22:371-375.
    • (2003) J Protein Chem , vol.22 , pp. 371-375
    • Yan, S.1    Liu, L.2    Tian, X.3    Zhang, Y.4    Zhou, H.5
  • 35
    • 0000925702 scopus 로고
    • Optimal conditions for the determination of serum alkaline phosphatase by a new kinetic method
    • Hausamen T.U., Helgar R., Rick W., Gross W. Optimal conditions for the determination of serum alkaline phosphatase by a new kinetic method. Clin Chim Acta 1967, 15:241-245.
    • (1967) Clin Chim Acta , vol.15 , pp. 241-245
    • Hausamen, T.U.1    Helgar, R.2    Rick, W.3    Gross, W.4
  • 36
    • 0015294205 scopus 로고
    • Study of optimum buffer conditions for measuring alkaline phosphatase activity in human serum
    • McComb R.B., Bowers G.N. Study of optimum buffer conditions for measuring alkaline phosphatase activity in human serum. Clin Chem 1972, 18:97-104.
    • (1972) Clin Chem , vol.18 , pp. 97-104
    • McComb, R.B.1    Bowers, G.N.2
  • 37
    • 0028934464 scopus 로고
    • Dependence of the phosphorylation of alkaline phosphatase by phosphate monoesters on the pKa of the leaving group
    • Han R., Colman J.E. Dependence of the phosphorylation of alkaline phosphatase by phosphate monoesters on the pKa of the leaving group. Biochemistry 1995, 34:4238-4245.
    • (1995) Biochemistry , vol.34 , pp. 4238-4245
    • Han, R.1    Colman, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.