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Volumn 122, Issue 4, 1997, Pages 779-787

Alanyl aminopeptidase from human seminal plasma: Purification characterization, and immunohistochemical localization in the male genital tract

Author keywords

Alanyl aminopeptidase; Characterization; Immunohistochemistry; Purification; Seminal plasma

Indexed keywords

1,10 PHENANTHROLINE; ACTINONIN; AMASTATIN; BESTATIN; COMPLEMENTARY DNA; ENZYME INHIBITOR; MERCAPTOETHANOL; MICROSOMAL AMINOPEPTIDASE; MONOMER;

EID: 0030679556     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021823     Document Type: Article
Times cited : (43)

References (36)
  • 1
    • 0028359970 scopus 로고
    • Effects of the synthetic glucocorticoid triamcinolone acetonide on vasoactive hydrolases of the human placenta in vitro
    • Hahn, T., Graf, R., Oney, T., and Desoye, G. (1994) Effects of the synthetic glucocorticoid triamcinolone acetonide on vasoactive hydrolases of the human placenta in vitro. Placenta 15, 377-388
    • (1994) Placenta , vol.15 , pp. 377-388
    • Hahn, T.1    Graf, R.2    Oney, T.3    Desoye, G.4
  • 2
    • 0025008623 scopus 로고
    • Characterization of aminopeptidases in human kindey soluble fraction
    • Mantle, D., Lauffart, B., McDermott, J., and Gibson, A. (1990) Characterization of aminopeptidases in human kindey soluble fraction. Clin. Chim. Acta 187, 105-114
    • (1990) Clin. Chim. Acta , vol.187 , pp. 105-114
    • Mantle, D.1    Lauffart, B.2    McDermott, J.3    Gibson, A.4
  • 3
    • 0028821377 scopus 로고
    • An aminopeptidase activity from porcine kidney that hydrolyzes oxytocin and vasopressin: Purification and partial characterization
    • Itoh, C. and Nagamatsu, A. (1995) An aminopeptidase activity from porcine kidney that hydrolyzes oxytocin and vasopressin: purification and partial characterization. Biochim. Biophys. Acta 1243, 203-208
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 203-208
    • Itoh, C.1    Nagamatsu, A.2
  • 4
    • 0024502582 scopus 로고
    • Comparison of major cortical aminopeptidase activity in normal brain and brain from patients with Alzheimer's disease
    • Mantle, D., Lauffart, B., Perry, E.K., and Perry, R.H. (1989) Comparison of major cortical aminopeptidase activity in normal brain and brain from patients with Alzheimer's disease. J. Neurol. Sci 89, 227-234
    • (1989) J. Neurol. Sci , vol.89 , pp. 227-234
    • Mantle, D.1    Lauffart, B.2    Perry, E.K.3    Perry, R.H.4
  • 5
    • 0028983163 scopus 로고
    • Decrease in cytosolic aspartyl-aminopeptidase but not in alanyl-aminopeptidase activity in the frontal cortex of the aged rat
    • Iribar, C., Esteban, M.J., Martinez, J.M., and Peinado, J.M. (1995) Decrease in cytosolic aspartyl-aminopeptidase but not in alanyl-aminopeptidase activity in the frontal cortex of the aged rat. Brain Res. 687, 211-213
    • (1995) Brain Res. , vol.687 , pp. 211-213
    • Iribar, C.1    Esteban, M.J.2    Martinez, J.M.3    Peinado, J.M.4
  • 6
    • 0018875451 scopus 로고
    • Multiple molecular forms of human pancreas alanine aminopeptidase
    • Sidorowicz, W., Jackson, G.G., and Behal, F.J. (1980) Multiple molecular forms of human pancreas alanine aminopeptidase. Clin. Chim. Acta 104, 169-179
    • (1980) Clin. Chim. Acta , vol.104 , pp. 169-179
    • Sidorowicz, W.1    Jackson, G.G.2    Behal, F.J.3
  • 7
    • 0023677326 scopus 로고
    • Rationalization of aminopeptidase activities in human skeletal muscle soluble extract
    • Lauffart, B. and Mantle, D. (1988) Rationalization of aminopeptidase activities in human skeletal muscle soluble extract. Biochim. Biophys. Acta 956, 300-306
    • (1988) Biochim. Biophys. Acta , vol.956 , pp. 300-306
    • Lauffart, B.1    Mantle, D.2
  • 9
    • 0022922648 scopus 로고
    • Characterization of three aminopeptidases purified from maternal serum
    • Lalu, K., Lampelo, S., and Vanha-Perttula, T. (1986) Characterization of three aminopeptidases purified from maternal serum. Biochim. Biophys. Acta 873, 190-197
    • (1986) Biochim. Biophys. Acta , vol.873 , pp. 190-197
    • Lalu, K.1    Lampelo, S.2    Vanha-Perttula, T.3
  • 10
    • 0022438888 scopus 로고
    • Alanyl aminopeptidase of bovine seminal vesicle secretion
    • Agrawal, Y. and Vanha-Perttula, T. (1986) Alanyl aminopeptidase of bovine seminal vesicle secretion. Int. J. Biochem. 18, 725-729
    • (1986) Int. J. Biochem. , vol.18 , pp. 725-729
    • Agrawal, Y.1    Vanha-Perttula, T.2
  • 11
    • 0023759290 scopus 로고
    • Purification and characterization of human seminal plasma aminopeptidase
    • NagDas, S.K. and Bhattacharyya, A.K. (1988) Purification and characterization of human seminal plasma aminopeptidase. Ital. J. Biochem. 37, 148-164
    • (1988) Ital. J. Biochem. , vol.37 , pp. 148-164
    • NagDas, S.K.1    Bhattacharyya, A.K.2
  • 12
    • 0026655048 scopus 로고
    • Purification and properties of an aminopeptidase from rat-liver cytosol
    • Hiroi, Y., Endo, Y., and Natori, Y. (1992) Purification and properties of an aminopeptidase from rat-liver cytosol. Arch. Biochem. Biophys. 294, 440-445
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 440-445
    • Hiroi, Y.1    Endo, Y.2    Natori, Y.3
  • 14
    • 0024511780 scopus 로고
    • Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N
    • Watt, V.M. and Yip, C.C. (1989) Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N. J. Biol. Chem. 264, 5480-5487
    • (1989) J. Biol. Chem. , vol.264 , pp. 5480-5487
    • Watt, V.M.1    Yip, C.C.2
  • 15
    • 0024358644 scopus 로고
    • Molecular cloning and amino acid sequence of rat kidney aminopeptidase M: A member of a super family of zinc-metallohydrolases
    • Malfroy, B., Kado-Fong, H., Gros, C., Giros, B., Schwartz, J.C., and Hellmiss, R. (1989) Molecular cloning and amino acid sequence of rat kidney aminopeptidase M: a member of a super family of zinc-metallohydrolases. Biochem. Biophys. Res. Commun. 161, 236-241
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 236-241
    • Malfroy, B.1    Kado-Fong, H.2    Gros, C.3    Giros, B.4    Schwartz, J.C.5    Hellmiss, R.6
  • 16
    • 0024518875 scopus 로고
    • Human myeloid plasma membrane glycoprotein CD 13 (gp 150) is identical to aminopeptidase N
    • Look, A.T., Ashmun, R.A., Shapiro, L.H., and Peiper, S.C. (1989) Human myeloid plasma membrane glycoprotein CD 13 (gp 150) is identical to aminopeptidase N. J. Clin. Invest. 83, 1299-1307
    • (1989) J. Clin. Invest. , vol.83 , pp. 1299-1307
    • Look, A.T.1    Ashmun, R.A.2    Shapiro, L.H.3    Peiper, S.C.4
  • 17
    • 0027971959 scopus 로고
    • Dipeptidyl peptidase IV from porcine seminal plasma: Purification, characterization and N-terminal amino acid sequence
    • Ohkubo, I., Huang, K., Ochiai, Y., Takagaki, M., and Kani, K. (1994) Dipeptidyl peptidase IV from porcine seminal plasma: purification, characterization and N-terminal amino acid sequence. J. Biochem. 116, 1182-1186
    • (1994) J. Biochem. , vol.116 , pp. 1182-1186
    • Ohkubo, I.1    Huang, K.2    Ochiai, Y.3    Takagaki, M.4    Kani, K.5
  • 18
    • 0030011385 scopus 로고    scopus 로고
    • Dipeptidyl peptidase II from porcine seminal plasma: Purification, characterization, and its homology to granzymes, cytotoxic cell proteinases (CCP 1-4)
    • Huang, K., Takagaki, M., Kani, K., and Ohkubo, I. (1996) Dipeptidyl peptidase II from porcine seminal plasma: purification, characterization, and its homology to granzymes, cytotoxic cell proteinases (CCP 1-4). Biochim. Biophys. Acta 1290, 149-156
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 149-156
    • Huang, K.1    Takagaki, M.2    Kani, K.3    Ohkubo, I.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0024516896 scopus 로고
    • Primary structure of rat liver dipeptidyl peptidase IV deduced from its cDNA and identification of the NH2-terminal signal sequence as the membrane-anchoring domain
    • Ogata, S., Misumi, Y., and Ikehara, Y. (1989) Primary structure of rat liver dipeptidyl peptidase IV deduced from its cDNA and identification of the NH2-terminal signal sequence as the membrane-anchoring domain. J. Biol. Chem. 264, 3596-3601
    • (1989) J. Biol. Chem. , vol.264 , pp. 3596-3601
    • Ogata, S.1    Misumi, Y.2    Ikehara, Y.3
  • 21
    • 0024321837 scopus 로고
    • Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography
    • (Fleischer, S. and Fleischer, B., eds.) Academic Press, San Diego
    • Hayashi, Y., Matsui, H., and Takagi, T. (1989) Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography in Methods in Enzymology (Fleischer, S. and Fleischer, B., eds.) Vol. 172, pp. 514-528, Academic Press, San Diego
    • (1989) Methods in Enzymology , vol.172 , pp. 514-528
    • Hayashi, Y.1    Matsui, H.2    Takagi, T.3
  • 22
    • 0027329037 scopus 로고
    • Purification of 3,5-dichlorocatechol 1,2-dioxygenase, a nonheme iron dioxygenase and a key enzyme in the biodegradation of a herbicide, 2,4-dichlorophenoxy acetic acid (2,4-D), from Pseudomonas cepacia CSV90
    • Bhat, M.A., Ishida, T., Horiike, K., Vaidyanathan, C.S., and Nozaki, M. (1993) Purification of 3,5-dichlorocatechol 1,2-dioxygenase, a nonheme iron dioxygenase and a key enzyme in the biodegradation of a herbicide, 2,4-dichlorophenoxy acetic acid (2,4-D), from Pseudomonas cepacia CSV90. Arch. Biochem. Biophys. 300, 738-746
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 738-746
    • Bhat, M.A.1    Ishida, T.2    Horiike, K.3    Vaidyanathan, C.S.4    Nozaki, M.5
  • 23
    • 0022426981 scopus 로고
    • Determination of absorbance coefficients of purified proteins by conventional ultraviolet spectrophotometry and chromatography combined with multiwavelength detection
    • van Iersel, J., Jzn, J.F., and Duine, J. A. (1985) Determination of absorbance coefficients of purified proteins by conventional ultraviolet spectrophotometry and chromatography combined with multiwavelength detection. Anal. Biochem. 151, 196-204
    • (1985) Anal. Biochem. , vol.151 , pp. 196-204
    • Van Iersel, J.1    Jzn, J.F.2    Duine, J.A.3
  • 24
    • 0013797229 scopus 로고
    • Immunochemical quantitation of antigens by single radial immunodiffusion
    • Mancini, G., Carbonara, A.O., and Heremans, J.F. (1965) Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry 2, 235-254
    • (1965) Immunochemistry , vol.2 , pp. 235-254
    • Mancini, G.1    Carbonara, A.O.2    Heremans, J.F.3
  • 26
    • 0025169326 scopus 로고
    • Identification and characterization of the major stilbene-disulphonate- and concanavalin A-binding protein of the porcine renal brush-border membrane as aminopeptidase N
    • See, H. and Reithmeir, R.A. (1990) Identification and characterization of the major stilbene-disulphonate-and concanavalin A-binding protein of the porcine renal brush-border membrane as aminopeptidase N. Biochem. J. 271, 147-155
    • (1990) Biochem. J. , vol.271 , pp. 147-155
    • See, H.1    Reithmeir, R.A.2
  • 27
    • 0027892641 scopus 로고
    • CD 13 (GP 150; aminopeptidase-N): Predominant functional activity in blood is localized to plasma and is not cell-surface associated
    • Favaloro, E.J., Browning, T., and Facey, D. (1993) CD 13 (GP 150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated. Exp. Hematol. 21, 1695-1701
    • (1993) Exp. Hematol. , vol.21 , pp. 1695-1701
    • Favaloro, E.J.1    Browning, T.2    Facey, D.3
  • 28
    • 0027461740 scopus 로고
    • Biochemical and functional characterization of aminopeptidase N expressed by human melanoma cells
    • Menrad, A., Speicher, D., Wacker, J., and Herlyn, M. (1993) Biochemical and functional characterization of aminopeptidase N expressed by human melanoma cells. Cancer Res. 53, 1450-1455
    • (1993) Cancer Res. , vol.53 , pp. 1450-1455
    • Menrad, A.1    Speicher, D.2    Wacker, J.3    Herlyn, M.4
  • 29
    • 0025057536 scopus 로고
    • Comparison of the soluble and membrane-bound forms of the puromycin-sensitive enkephalin-degrading aminopeptidase from rat
    • Dyer, S.H., Slaughter, C.A., Orth, K., Moomaw, C.R., and Hersh, L.B. (1990) Comparison of the soluble and membrane-bound forms of the puromycin-sensitive enkephalin-degrading aminopeptidase from rat. J. Neurochem. 54, 547-554
    • (1990) J. Neurochem. , vol.54 , pp. 547-554
    • Dyer, S.H.1    Slaughter, C.A.2    Orth, K.3    Moomaw, C.R.4    Hersh, L.B.5
  • 30
    • 0028843821 scopus 로고
    • Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and founctional characterization
    • Constam, D.B., Tobler, A.R., Rensing-Ehl, A., Kemler, I., Hersh, L.B., and Fontana, A. (1995) Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and founctional characterization. J. Biol. Chem. 270, 26931-26936
    • (1995) J. Biol. Chem. , vol.270 , pp. 26931-26936
    • Constam, D.B.1    Tobler, A.R.2    Rensing-Ehl, A.3    Kemler, I.4    Hersh, L.B.5    Fontana, A.6
  • 31
    • 0022006475 scopus 로고
    • The metabolism of neuropeptidase phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N
    • Matsas, R., Stephenson, S.L., Hryszko, J., Kenny, A.J., and Turner, A.J. (1985) The metabolism of neuropeptidase phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N. Biochem. J. 231, 445-449
    • (1985) Biochem. J. , vol.231 , pp. 445-449
    • Matsas, R.1    Stephenson, S.L.2    Hryszko, J.3    Kenny, A.J.4    Turner, A.J.5
  • 32
    • 0023156650 scopus 로고
    • An immunohistochemical study of endopeptidase-24.11 and aminopeptidase N in lymphoid tissues
    • Bowes, M.A. and Kenny, A.J. (1987) An immunohistochemical study of endopeptidase-24.11 and aminopeptidase N in lymphoid tissues. Immunology 60, 247-253
    • (1987) Immunology , vol.60 , pp. 247-253
    • Bowes, M.A.1    Kenny, A.J.2
  • 33
    • 0026729302 scopus 로고
    • Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV
    • Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Norén, O., and Laude, H. (1992) Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV. Nature 357, 417-420
    • (1992) Nature , vol.357 , pp. 417-420
    • Delmas, B.1    Gelfi, J.2    L'Haridon, R.3    Vogel, L.K.4    Sjöström, H.5    Norén, O.6    Laude, H.7
  • 36
    • 0023095257 scopus 로고
    • Enzyme activities of human seminal plasma having different states of coagulation
    • NagDas, S.K. and Bhattacharyya, A.K. (1987) Enzyme activities of human seminal plasma having different states of coagulation. Int. J. Fertil. 32, 86-89
    • (1987) Int. J. Fertil. , vol.32 , pp. 86-89
    • Nagdas, S.K.1    Bhattacharyya, A.K.2


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