| Literature DB >> 393604 |
D Cechová, V Jonáková, E Sedláková, O Mach.
Abstract
An acrosin inhibitor was isolated from bull seminal plasma by gel filtration on Sephadex G-50 fine and ion-exchange chromatography on CM-Sephadex. The inhibitor is a basic polypeptide (pl greater than or equal to 10.5) of molecular weight 6 200 (calculated from amino acid composition). Its N-terminal amino group is blocked. The inhibitor is not strictly specific in its effect since it also inhibits trypsin and to a lesser degree chymotrypsin, in addition to bull and boar acrosin.Entities:
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Year: 1979 PMID: 393604 DOI: 10.1515/bchm2.1979.360.2.1753
Source DB: PubMed Journal: Hoppe Seylers Z Physiol Chem ISSN: 0018-4888