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The 145‐fold purification of a proteolytic enzyme from human spermatozoa by chromatography on SP‐Sephadex and Sephadex G‐100 is described. The enzyme possesses a molecular weight of 76000 ± 4000, exists as a monomer in solution and consists of a single polypeptide chain. As judged by its inhibition spectrum, substrate specificity and pH‐activity curve it is a trypsinlike enzyme. When initial velocity was measured against substrate concentration, a slight cooperative effect was observed. The enzyme is stable at pH 3.2 and labile at pH 8.1. At this pH, Mn 2+ , Mg 2+ or Ca 2+ ions have no effect on its activity or stability. It is identified as human acrosin.
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Gilboa et al. (1973) studied this question.
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