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Acrosin shows zona and fucose binding, novel properties for a serine proteinase
Author(s) -
Töpfer-Petersen E.,
Henschen A.
Publication year - 1987
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(87)80546-x
Subject(s) - acrosin , zona pellucida , biochemistry , serine , chemistry , zona pellucida glycoprotein , boar , affinity chromatography , avidin , sperm , biology , microbiology and biotechnology , biotinylation , enzyme , oocyte , acrosome , embryo , botany
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.