Acrosin inhibition. Comparisons of membrane-associated and -solubilized enzyme.

作者: J W Straus , K L Polakoski

DOI: 10.1016/S0021-9258(18)34281-9

关键词:

摘要: Acrosin is an extrinsic membrane proteinase from spermatozoa which functions in the fertilization process. Liposomes were utilized as a model system to determined possible effects of association on acrosin's enzymatic activity. By comparison with solubilized enzyme, liposome-bound acrosin had substantial reduction apparent affinity for "progressive" inhibitors such leupeptin, lima bean trypsin inhibitor, soy and inhibitor sperm extracts. In contrast, -solubilized enzymes essentially identical respect binding benzamidine p-aminobenzamidine are competitive inhibitors. These results suggest can influence some but not all properties.

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