Töpfer-Petersen E, Steinberger M, von Eschenbach C E, Zucker A
Department of Dermatology, University of Munich, FRG.
FEBS Lett. 1990 Jun 4;265(1-2):51-4. doi: 10.1016/0014-5793(90)80881-i.
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.
