Purification and characterization of β‐glucuronidase from bull seminal plasma and its role in fertilization

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Abstract
Bull seminal plasma contains high levels of β‐glucuronidase. The present study describes the isolation and characterization of β‐glucuronidase, and its role in fertilization. β‐glucuronidase was purified by ion exchange chromatography, saccharolactone‐agarose affinity chromatography, and gel filtration. The specific activity of the purified enzyme was 4,414 μmoles/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 Mr 75,000 each. The apparent Km and Vmax for β‐glucuronidase were 0.4 mM and 5.7 μmol/min using phenolpthalein mono‐β‐glucuronic acid as the substrate. β‐glucuronidase appeared to accelerate the cumulus dispersion in vitro.