Open AccessPurification and Properties of Human Acrosin
Author(s) -
Gilboa Eli,
Elkana Yehudit,
Rigbi Meir
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb03106.x
Subject(s) - sephadex , chemistry , enzyme , acrosin , substrate (aquarium) , chromatography , monomer , enzyme assay , biochemistry , biology , organic chemistry , ecology , semen , acrosome , genetics , polymer
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.