Identification of 17–18 kDa zona pellucida binding proteins from boar spermatozoa
- 21 May 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 264 (2) , 243-245
- https://doi.org/10.1016/0014-5793(90)80258-k
Abstract
Zona pellucida (ZP) binding proteins from boar spermatozoa were compared with antigens recognized by ACR.2 and ACR.3 monoclonal antibodies. The ZP binding proteins of 55, 53,45 and 38 kDa are identical with various forms of boar acrosin immunologically detected by ACR.2 antibody. The ZP binding proteins of 17 and 18 kDa are recognized by ACR.3 antibody. The N‐tenninal amino acid sequence of the 17 kDa protein revealed that it is not derived from an acrosin molecule.Keywords
This publication has 15 references indexed in Scilit:
- Molecular cloning of preproacrosin and analysis of its expression pattern in spermatogenesisEuropean Journal of Biochemistry, 1989
- Sperm‐egg recognition and barriers to interspecies fertilizationGamete Research, 1988
- Zona Pellucida-Binding and Fucose-Binding of Boar Sperm Acrosin is Not Correlated with Proteolytic ActivityBiological Chemistry Hoppe-Seyler, 1988
- Acrosin shows zona and fucose binding, novel properties for a serine proteinaseFEBS Letters, 1987
- The Biology and Chemistry of FertilizationScience, 1987
- Protein-blotting on Polybrene-coated glass-fiber sheets. A basis for acid hydrolysis and gas-phase sequencing of picomole quantities of protein previously separated on sodium dodecyl sulfate/polyacrylamide gelEuropean Journal of Biochemistry, 1985
- Identification of zona binding proteins of rabbit, pig, human, and mouse spermatozoa on nitrocellulose blotsJournal of Experimental Zoology, 1985
- Sensitive colloidal metal (gold or silver) staining of protein blots on nitrocellulose membranesAnalytical Biochemistry, 1985
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970