Purification and Properties of Human Acrosin

Eli Gilboa, Yehudit Elkana, Meir Rigbi

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


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 languageEnglish (US)
Pages (from-to)85-92
Number of pages8
JournalEuropean Journal of Biochemistry
Issue number1
StatePublished - Nov 1973
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


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