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A new acrosin inhibitor was isolated to apparent homogeneity from the fluid of boar seminal vesicles. The inhibitor is immunologically related to the polyvalent trypsin-kallikrein inhibitor from bovine lung known as aprotinin. A crude preparation of the acrosin inhibitor was prepared by immunoaffinity chromatography on anti-aprotinin antibodies bound to Sepharose 4B column. The inhibitor was further purified by affinity chromatography on trypsin immobilized on a Sepharose 4B column, by ion-exchange chromatography on CM-Sephadex C-25, and by reversed-phase high-performance liquid chromatography on a C18 column. The relative molecular mass (Mr) of the inhibitor is about 7,000 as estimated from dodecyl sulfate-polyacrylamide gel electrophoresis. Its amino-acid composition was determined, the sequence of the first 8 amino-acid residues from the N-terminus is Thr-Arg-Asp-Phe-Pro-Pro-Asp-Gly-...
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D Cechová, and
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L Veselský
June 1972,
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V Jonáková, and
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V Jonáková, and
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V Jonáková, and
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V Jonáková, and
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V Jonáková, and
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V Jonáková, and
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V Jonáková, and
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L Veselský
January 2016,
International journal of biological macromolecules,
