Zona pellucida-binding of boar sperm acrosin is associated with the N-terminal peptide of the acrosin B-chain (heavy chain).
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 (55/53 kDa), designated as alpha-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 zona-binding 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.
Töpfer-Petersen
E
E
Department of Dermatology, University of Munich, FRG.
Steinberger
M
M
von Eschenbach
C E
CE
Zucker
A
A
D000176:Acrosin / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D005260:Female; D046911:Macromolecular Substances; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010063:Ovum / Q000378:metabolism*; D011485:Protein Binding; D012697:Serine Endopeptidases / Q000378:metabolism*; D013094:Spermatozoa / Q000201:enzymology; D013552:Swine; D015044:Zona Pellucida / Q000378:metabolism*
D046911:Macromolecular Substances; D012697:Serine Endopeptidases; D000176:Acrosin