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Multiple Forms of Boar Acrosin and their Relationship to Proenzyme Activation by Wolf-Dieter SCHLEUNING; Ruža HELL; Hans FRITZ is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Further evidence is presented that the acrosomal proteinase acrosin exists as a zymogen precursor in freshly ejaculated boar spermatozoa. Autoactivation of proacrosin to acrosin takes place optimally at slightly alkaline pH and in the presence of calcium ions. Activation is considerably accelerated by catalytic amounts of trypsin or highly purified acrosin. A significant acceleration of the activation is also achieved by porcine pancreatic and urinary kallikrein, whereas chymotrypsin, plasmin, thrombin or urokinase showed no effect. Activation can be inhibited by p-amino-benzamidine and p-nitrophenyl p'-guanidino-benzoate. Electrophoretic analysis at different stages of activation revealed that during this process various molecular forms of acrosin are produced, apparently by limited proteolysis.

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Author

Wolf-Dieter SCHLEUNING; Ruža HELL; Hans FRITZ

Publisher

Walter de Gruyter GmbH

Published

1976

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)