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Proacrosin was extracted from freshly ejaculated bull and ram spermatozoa with acidic buffer solution pH 3.0, and was partially purified by gel filtration to remove acrosin inhibitors. The occurrence of multiple active forms during proacrosin activation at pH 7.8 was monitored by active enzyme staining of samples after polyacrylamide gel electrophoresis at pH 3.8. For comparison, the protein pattern of such activation samples was also determined after sodium dodecylsulfate-polyacrylamide gel electrophoresis. Proacrosin activation was completely prevented in the presence of 10(-4) M p-nitrophenyl p'-guanidinobenzoate.

hoppe-seyler's zeitschrift für physiologische chemie

Occurrence of Multiple Forms of Bull and Ram Acrosin during Proenzyme Activation and Inhibition of Activation by  p -Nitrophenyl  p ’-guanidinobenzoate