Acrosin shows zona and fucose binding, novel properties for a serine proteinase

FEBS Letters

Henschen, A.¹  Töpfer-Petersen, E.¹ 

[1] Department of Dermatology, Andrology Unit, University of Munich, Frauenlobstr. 9/11, 8000 Munich 2 and Max Planck Institute for Biochemistry, 8033 Martinsried, FRG

关键词: Zona binding;    Fucose binding;    Acrosin;    Sperm-zona interaction;    (Boar spermatozoon);    HPLC;    high-performance liquid chromatography;    FPLC;    fast-protein liquid chromatography;   

DOI  :  10.1016/0014-5793(87)80546-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The major fucose-binding protein of 53 kDa from boar spermatozoa was isolated to apparent homogeneity using a two-step procedure including high-performance gel filtration and reversed-phase chromatography. The N-terminal sequence of the protein revealed that it is identical with the sperm proteinase acrosin. By means of a solid-phase zona-binding assay based on the avidin-biotin system it was demonstrated that acrosin also interacts strongly with porcine zona pellucida. Thus, the acrosin molecule combines specific proteolytic activity with zona- and carbohydrate-affinity properties, i.e. previously unrecognized properties of a serine proteinase. It seems likely that this special affinity of acrosin directs the proteolytic activity to its structural target in the in vivo situation.

【 授权许可】

Unknown