Variability of acrosin inhibitors in boar reproductive tract.
V Jonáková, Dana Cechova, Edda Töpfer‐Petersen, Juan J. Calvete, Leopold VESELSKÝ
Abstract
V Jonáková, Dana Cechova, Edda Töpfer‐Petersen, Juan J. Calvete, Leopold VESELSKÝ
Abstract
A new acrosin inhibitor with a relative molecular mass of about 8000 was isolated to apparent homogeneity from ejaculated boar spermatozoa. The inhibitor is effective against boar acrosin and bovine trypsin. It interacts with polyvalent antibodies against the acrosin inhibitor from boar seminal plasma, but differs from all known acrosin inhibitors in its amino acid composition and N-terminal sequence.
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A new acrosin inhibitor with a relative molecular mass of about 8000 was isolated to apparent homogeneity from ejaculated boar spermatozoa. The inhibitor is effective against boar acrosin and bovine trypsin. It interacts with polyvalent antibodies against the acrosin inhibitor from boar seminal plasma, but differs from all known acrosin inhibitors in its amino acid composition and N-terminal sequence.
Key concepts: Acrosin, BOAR, Chemistry, Reproductive tract, Trypsin, Biochemistry, Enzyme, Biology