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Volumn 12, Issue 1, 2001, Pages 107-111

Purification and partial peptide sequence analysis of the boar 32 kDa sperminogen

Author keywords

Acrosin; Proacrosin; Spermatozoa; Sperminogen

Indexed keywords

ACROSIN; ENZYME PRECURSOR; PEPTIDE FRAGMENT; PROACROSIN; SEMINAL PLASMA PROTEIN;

EID: 0035980106     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (24)
  • 1
    • 0028017503 scopus 로고
    • Purification and characterization of a novel acrosin-like enzyme from boar cauda epididymal sperm
    • Akama, K., Terao, K., Tanaka, Y., Noguchi, A., Yonezawa, N., Nakano, M., and Tobita, T. (1994) Purification and characterization of a novel acrosin-like enzyme from boar cauda epididymal sperm. J. Biochem. 116, 464-470.
    • (1994) J. Biochem. , vol.116 , pp. 464-470
    • Akama, K.1    Terao, K.2    Tanaka, Y.3    Noguchi, A.4    Yonezawa, N.5    Nakano, M.6    Tobita, T.7
  • 2
    • 0027948083 scopus 로고
    • Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization
    • Baba, T., Azuma, S., Kashiwabara, S., and Toyoda, Y. (1994) Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J. Biol. Chem. 269, 31845-31849.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31845-31849
    • Baba, T.1    Azuma, S.2    Kashiwabara, S.3    Toyoda, Y.4
  • 4
    • 84949404676 scopus 로고
    • Is sperminogen a modified proacrosin? Isolation, purification and partial characterization of low molecular mass boar proacrosin
    • Cechova, D., Topfer-Petersen, E., Zucker, A., and Jonakova, V. (1990) Is sperminogen a modified proacrosin? Isolation, purification and partial characterization of low molecular mass boar proacrosin. Biol. Chem. Hoppe-Seyler 371, 317-323.
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , pp. 317-323
    • Cechova, D.1    Topfer-Petersen, E.2    Zucker, A.3    Jonakova, V.4
  • 5
    • 0028216688 scopus 로고
    • Serine protease activity in boar seminal vesicles and its immunological similarity to sperm acrosin
    • Cechova, D., Jonakova, V., Veselsky, L., and Topfer-Petersen, E. (1994) Serine protease activity in boar seminal vesicles and its immunological similarity to sperm acrosin. J. Reprod. Fertil. 100, 461-467.
    • (1994) J. Reprod. Fertil. , vol.100 , pp. 461-467
    • Cechova, D.1    Jonakova, V.2    Veselsky, L.3    Topfer-Petersen, E.4
  • 7
    • 0032816742 scopus 로고    scopus 로고
    • Purification and partial peptide sequence analysis of the boar proacrosin binding protein
    • Huh, K. and Yi, L. S. (1999) Purification and partial peptide sequence analysis of the boar proacrosin binding protein. Mol. Reprod. Dev. 54, 76-80.
    • (1999) Mol. Reprod. Dev. , vol.54 , pp. 76-80
    • Huh, K.1    Yi, L.S.2
  • 8
  • 9
    • 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
  • 10
    • 0017126743 scopus 로고
    • Acrolysin, the aminoproteinase catalyzing the initial conversion of proacrosin to acrosin in mammalian fertilization
    • McRorie, R. S., Turner, R. B., Bradford, M. M., and Williams, W. L. (1976) Acrolysin, the aminoproteinase catalyzing the initial conversion of proacrosin to acrosin in mammalian fertilization. Biochem. Biophys. Res. Commun. 71, 492-498.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 492-498
    • McRorie, R.S.1    Turner, R.B.2    Bradford, M.M.3    Williams, W.L.4
  • 11
    • 0015455055 scopus 로고
    • Biochemical detection and activation of an inactive form of a trypsin-like enzyme in rabbit testes
    • Meizel, S. (1972) Biochemical detection and activation of an inactive form of a trypsin-like enzyme in rabbit testes. J. Reprod. Fertil. 31, 459-462.
    • (1972) J. Reprod. Fertil. , vol.31 , pp. 459-462
    • Meizel, S.1
  • 12
    • 0015295876 scopus 로고
    • Partial characterization of a new bull sperm arylamidase
    • Meizel, S. and Cotham, J. (1972) Partial characterization of a new bull sperm arylamidase. J. Reprod. Fertil. 28, 303-307.
    • (1972) J. Reprod. Fertil. , vol.28 , pp. 303-307
    • Meizel, S.1    Cotham, J.2
  • 13
    • 0027228101 scopus 로고
    • Protein-protein interactions controlling acrosin release nd solubilization during the boar sperm acrosome reaction
    • Moos, J., Peknicova, J., and Tesarik, J. (1993) Protein-protein interactions controlling acrosin release nd solubilization during the boar sperm acrosome reaction. Biol. Reprod. 49, 408-415.
    • (1993) Biol. Reprod. , vol.49 , pp. 408-415
    • Moos, J.1    Peknicova, J.2    Tesarik, J.3
  • 14
    • 0032883785 scopus 로고    scopus 로고
    • A homologue of pancreatic trypsin is localized in the acrosome of mammalian sperm and is released during acrosome reaction
    • Ohmura, K., Kohno, N., Kobayashi, Y., Yamagata, K., Sato, S., Kashiwabara, S., and Baba, T. (1999) A homologue of pancreatic trypsin is localized in the acrosome of mammalian sperm and is released during acrosome reaction. J. Biol. Chem. 274, 29426-29432.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29426-29432
    • Ohmura, K.1    Kohno, N.2    Kobayashi, Y.3    Yamagata, K.4    Sato, S.5    Kashiwabara, S.6    Baba, T.7
  • 15
    • 0021759356 scopus 로고
    • Purification and characterization of two types of trypsin-like enzymes from sperm of the ascidian (Prochordata) Halocynthia roretzi. Evidence for the presence of spermosin, a novel acrosin-like enzyme
    • Sawada, H., Yokosawa, H., and Ishii, S. (1984) Purification and characterization of two types of trypsin-like enzymes from sperm of the ascidian (Prochordata) Halocynthia roretzi. Evidence for the presence of spermosin, a novel acrosin-like enzyme. J. Biol. Chem. 259, 2900-2904.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2900-2904
    • Sawada, H.1    Yokosawa, H.2    Ishii, S.3
  • 16
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 17
    • 0023193930 scopus 로고
    • Partial purification and characterization of human sperminogen
    • Siegel, M. S., Bechtold, D. S., Willand, J. L., and Polakoski, K. L. (1987) Partial purification and characterization of human sperminogen. Biol. Reprod. 36, 1063-1068.
    • (1987) Biol. Reprod. , vol.36 , pp. 1063-1068
    • Siegel, M.S.1    Bechtold, D.S.2    Willand, J.L.3    Polakoski, K.L.4
  • 18
  • 20
    • 0031826659 scopus 로고    scopus 로고
    • The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization
    • Tulsiani, D. R., Abou-Haila, A., Loeser, C. R., and Pereira, B. M. (1998) The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization. Exp. Cell. Res. 240, 151-164.
    • (1998) Exp. Cell. Res. , vol.240 , pp. 151-164
    • Tulsiani, D.R.1    Abou-Haila, A.2    Loeser, C.R.3    Pereira, B.M.4
  • 21
    • 0032197525 scopus 로고    scopus 로고
    • p-Aminobenzamidine-sensitive acrosomal protease(s) other than acrosin serve the sperm penetration of the egg zona pellucida in mouse
    • Yamagata, K., Murayama, K., Kohno, N., Kashiwabara, S., and Baba, T., (1998) p-Aminobenzamidine-sensitive acrosomal protease(s) other than acrosin serve the sperm penetration of the egg zona pellucida in mouse. Zygote 6, 311-319.
    • (1998) Zygote , vol.6 , pp. 311-319
    • Yamagata, K.1    Murayama, K.2    Kohno, N.3    Kashiwabara, S.4    Baba, T.5
  • 22
    • 0031313577 scopus 로고    scopus 로고
    • Purification and partial immuno-characterization of boar sperm proteinase sperminogen
    • Yi, L. (1997) Purification and partial immuno-characterization of boar sperm proteinase sperminogen. J. Biochem. Mol. Biol. 30, 448-452.
    • (1997) J. Biochem. Mol. Biol. , vol.30 , pp. 448-452
    • Yi, L.1
  • 23
    • 0026583227 scopus 로고
    • Proacrosin binding protein: Immunocomparative studies in boar, bovine, hamster, human, and ram
    • Yi, L. S. and Polakoski, K. L. (1992) Proacrosin binding protein: immunocomparative studies in boar, bovine, hamster, human, and ram. J. Reprod. Immunol. 21, 309-320.
    • (1992) J. Reprod. Immunol. , vol.21 , pp. 309-320
    • Yi, L.S.1    Polakoski, K.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.