Zona pellucida‐binding of boar sperm acrosin is associated with the N‐terminal peptide of the acrosin B‐chain (heavy chain)

FEBS Letters

Steinberger, M.²  Zucker, A.¹  Ebner von Eschenbach, C.²  Töpfer-Petersen, E.² 

[1] Institute of Physiological Chemistry, University of Munich, Goethestraße 33, D-8000 München 2, FRG;Department of Dermatology, Andrology Unit, University of Munich, Frauenlobstraße 9/11, D-8000 Munich 2, FRG

关键词: Sperm-egg interaction;    Acrosin;    Zona-binding;    Amino acid sequence;    Spermatozoa;    FPLC;    fast protein liquid chromatography;    HPLC;    high-performance liquid chromatography;    SDS-PAGE;    sodium dodecylsulfate polyacrylamide electrophoresis;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(90)80881-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown