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Molecular reproduction and development

Purification and characterization of beta-glucuronidase from bull seminal plasma and its role in fertilization.


PMID 7980949

Abstract

Bull seminal plasma contains high levels of beta-glucuronidase. The present study describes the isolation and characterization of beta-glucuronidase, and its role in fertilization. beta-glucuronidase was purified by ion exchange chromatography, saccharolactone-agarose affinity chromatography, and gel filtration. The specific activity of the purified enzyme was 4,414 mumoles/mg protein/min. The purified enzyme showed a single band on 7.5% PAGE. On SDS-PAGE, the enzyme appeared to consist of four identical subunits of M(r) 75,000 each. The apparent Km and Vmax for beta-glucuronidase were 0.4 mM and 5.7 mumol/min using phenolpthalein mono-beta-glucuronic acid as the substrate. beta-glucuronidase appeared to accelerate the cumulus dispersion in vitro.