The 45 fold purification of a proteolytic enzyme from human spermatozoa by chromatography on SP Sephadex and Sephadex G 00 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, Mn2+, Mg2+ or Ca2+ ions have no effect on its activity or stability. It is identified as human acrosin.
|Original language||English (US)|
|Number of pages||8|
|Journal||European Journal of Biochemistry|
|State||Published - Nov 1973|
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