메뉴 건너뛰기




Volumn 44, Issue 3, 1998, Pages 93-96

Antibody against 28-kDa intra-acrosomal sperm protein as a tool for evaluation of acrosomal integrity in bull spermatozoa

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; CALCIMYCIN; CELL PROTEIN; MONOCLONAL ANTIBODY;

EID: 0040032448     PISSN: 00155500     EISSN: 25337602     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (19)
  • 1
    • 0020839737 scopus 로고
    • In vitro fertilization of bovine oocytes by spermatozoa capacitated in vitro
    • Bondioli, R., Wright, R. W. (1983) In vitro fertilization of bovine oocytes by spermatozoa capacitated in vitro. J. Anim. Sci. 57, 1001-1005.
    • (1983) J. Anim. Sci. , vol.57 , pp. 1001-1005
    • Bondioli, R.1    Wright, R.W.2
  • 2
    • 0022552266 scopus 로고
    • Autoradiographic visualization of the mouse egg's sperm receptor bound to sperm
    • Bleil, J. D., Wassarman, P. M. (1986) Autoradiographic visualization of the mouse egg's sperm receptor bound to sperm. J. Cell Biol. 102, 1363-1371.
    • (1986) J. Cell Biol. , vol.102 , pp. 1363-1371
    • Bleil, J.D.1    Wassarman, P.M.2
  • 3
    • 0030812293 scopus 로고    scopus 로고
    • Monoclonal antibodies to canine intra-acrosomal sperm proteins recognizing acrosomal status during capacitation and acrosome reaction
    • Geussová, G., Pěknicová, J., Čapková, J., Kaláb, P., Moos, J., Phillimonenko, V. V., Hozák, P. (1997) Monoclonal antibodies to canine intra-acrosomal sperm proteins recognizing acrosomal status during capacitation and acrosome reaction. Andrologia 29, 261-268.
    • (1997) Andrologia , vol.29 , pp. 261-268
    • Geussová, G.1    Pěknicová, J.2    Čapková, J.3    Kaláb, P.4    Moos, J.5    Phillimonenko, V.V.6    Hozák, P.7
  • 4
    • 0142160421 scopus 로고
    • Structure-function properties of the sperm enzyme acrosin
    • eds. Shoemaker, S., Sonnet, P., Whitaker, J., ACS Symposium Series, ACR Books, Washington
    • Hedrick, J. L., Urch, U. A., Hardy, D. M. (1988) Structure-function properties of the sperm enzyme acrosin. In: Enzymes in Agricultural Biotechnology, eds. Shoemaker, S., Sonnet, P., Whitaker, J., pp. 1-10. ACS Symposium Series, ACR Books, Washington.
    • (1988) Enzymes in Agricultural Biotechnology , pp. 1-10
    • Hedrick, J.L.1    Urch, U.A.2    Hardy, D.M.3
  • 5
    • 0023445722 scopus 로고
    • Evidence for boar sperm proacrosin as a carbohydrate binding protein
    • Jones, R. (1987) Evidence for boar sperm proacrosin as a carbohydrate binding protein. Cell Biol Int. Rep. 11, 833.
    • (1987) Cell Biol Int. Rep. , vol.11 , pp. 833
    • Jones, R.1
  • 6
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bactcriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of the bactcriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 7
    • 0012141131 scopus 로고
    • A possible biological role of boar sperm diapharose investigated by a specific monoclonal antibody
    • Mollova, M., Atanasov, B., Ivanova, M., Kyurkchiev, S. (1992) A possible biological role of boar sperm diapharose investigated by a specific monoclonal antibody. Anim. Reprod. Sci. 29, 275-288.
    • (1992) Anim. Reprod. Sci. , vol.29 , pp. 275-288
    • Mollova, M.1    Atanasov, B.2    Ivanova, M.3    Kyurkchiev, S.4
  • 8
    • 0027228101 scopus 로고
    • Protein-protein interaction controlling acrosin release and solubilization during the boar sperm acrosome reaction
    • Moos, J., Pěknicová, J., Tesarik, J. (1993) Protein-protein interaction controlling acrosin release and solubilization during the boar sperm acrosome reaction. Biol. Reprod. 49, 408-415.
    • (1993) Biol. Reprod. , vol.49 , pp. 408-415
    • Moos, J.1    Pěknicová, J.2    Tesarik, J.3
  • 9
    • 0018396242 scopus 로고
    • Mammalian sperm proacrosin-acrosin system
    • Parish, R. F., Polakoski, K. I. (1979) Mammalian sperm proacrosin-acrosin system. Int. J. Biochem. 10, 391-395.
    • (1979) Int. J. Biochem. , vol.10 , pp. 391-395
    • Parish, R.F.1    Polakoski, K.I.2
  • 10
    • 0025647001 scopus 로고
    • Monoclonal antibodies against boar acrosomal antigens labelling undamaged acrosomes of spermatozoa in immunofluorescence test
    • Pěknicová, J., Moos, J. (1990) Monoclonal antibodies against boar acrosomal antigens labelling undamaged acrosomes of spermatozoa in immunofluorescence test. Andrologia 22, 427-435.
    • (1990) Andrologia , vol.22 , pp. 427-435
    • Pěknicová, J.1    Moos, J.2
  • 11
    • 0027975776 scopus 로고
    • Changes in immunochemical localisation of acrosomal and sperm proteins in boar spermatozoa during capacitation and induced acrosome reaction
    • Pěknicová, J., Moos, J., Mollova, M., Sršeň, V., Čapková, J. (1994) Changes in immunochemical localisation of acrosomal and sperm proteins in boar spermatozoa during capacitation and induced acrosome reaction. Arum. Reprod. Sci. 35, 255-271.
    • (1994) Arum. Reprod. Sci. , vol.35 , pp. 255-271
    • Pěknicová, J.1    Moos, J.2    Mollova, M.3    Sršeň, V.4    Čapková, J.5
  • 12
    • 0023735697 scopus 로고
    • Subcellular immunochemical localization of acrosin in human spermatozoa during the acrosome reaction and zona pellucida penetration
    • Tesarik, J., Drahorád, J., Pěknicová, J. (1988) Subcellular immunochemical localization of acrosin in human spermatozoa during the acrosome reaction and zona pellucida penetration. Fertil. Steril. 50, 133-141.
    • (1988) Fertil. Steril. , vol.50 , pp. 133-141
    • Tesarik, J.1    Drahorád, J.2    Pěknicová, J.3
  • 13
    • 0023662092 scopus 로고
    • Acrosin shows zona and fucose binding, novel properties for a serine proteinase
    • Töpfer-Petersen, E., Henschen, A. (1987) Acrosin shows zona and fucose binding, novel properties for a serine proteinase. FEBS Lett. 226, 38-42.
    • (1987) FEBS Lett. , vol.226 , pp. 38-42
    • Töpfer-Petersen, E.1    Henschen, A.2
  • 14
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications
    • Towbin, H., Staehelin, T., Gordon, G. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, G.3
  • 15
    • 0027297159 scopus 로고
    • Molecular events mediating sperm activation
    • Ward, C. R., Kopf, G. S. (1993) Molecular events mediating sperm activation. Dev. Biol. 158, 9-34.
    • (1993) Dev. Biol. , vol.158 , pp. 9-34
    • Ward, C.R.1    Kopf, G.S.2
  • 16
    • 0023515850 scopus 로고
    • Early events in mammalian fertilization
    • Wassarman, P. M. (1987) Early events in mammalian fertilization. Annu. Rev. Cell Biol. 3, 109-142.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 109-142
    • Wassarman, P.M.1
  • 17
    • 0026583227 scopus 로고
    • Proacrosin binding protein: Immunocomparative studies in boar, bovine, hamster, human, and ram
    • Yi, L.S.H., 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.H.1    Polakoski, K.L.2
  • 18
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • eds. Knobil, E., Neil, J., Raven Press, New York
    • Yanagimachi, R. (1994) Mammalian fertilization. In: The Physiology of Reproduction, eds. Knobil, E., Neil, J., pp. 81-182, Raven Press, New York.
    • (1994) The Physiology of Reproduction , pp. 81-182
    • Yanagimachi, R.1
  • 19
    • 0020164503 scopus 로고
    • Boar acrosin. Isolation of two active forms from boar ejaculated sperm
    • Železná, B., Čechová, D. (1982) Boar acrosin. Isolation of two active forms from boar ejaculated sperm. Hoppe-Seyler's Z. Physiol. Chem. 363, 757-776.
    • (1982) Hoppe-Seyler's Z. Physiol. Chem. , vol.363 , pp. 757-776
    • Železná, B.1    Čechová, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.