Premium
Zona pellucida‐binding of boar sperm acrosin is associated with the N‐terminal peptide of the acrosin B‐chain (heavy chain)
Author(s) -
Töpfer-Petersen E.,
Steinberger M.,
Ebner von Eschenbach C.,
Zucker A.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80881-i
Subject(s) - acrosin , zona pellucida , zona pellucida glycoprotein , chemistry , peptide , boar , biochemistry , oocyte , sperm , biology , acrosome , microbiology and biotechnology , genetics , embryo
Recently, it has been shown that boar acrosin exhibits a carbohydrate‐binding activity with a specificity to fucose, by which it can bind to the oocyte zona pellucida. By limited autoproteolysis of a high‐molecular mass acrosin (kDa), designated as α‐acrosin, a 15 kDa fragment was generated which interacts strongly with the porcine zona pellucida. Zona‐binding was demonstrated on protein blots and by the solid‐phase zonabinding assay utilizing biotinylated zona proteins. The zona‐binding peptide was isolated by reversed‐phase HPLC and analyzed for amino acid sequence. Its single N‐terminal sequence corresponded to that of the acrosin B‐chain (heavy chain). These data indicate that the zona‐binding properties of acrosin are associated with the N‐terminal peptide of the acrosin heavy chain.