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Purification and characterization of β‐glucuronidase from bull seminal plasma and its role in fertilization
Author(s) -
Rethinaswamy Asokan,
Yang ChulHak,
Srivastava Prakash N.
Publication year - 1994
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.1080380408
Subject(s) - biology , human fertilization , andrology , microbiology and biotechnology , genetics , medicine
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 M r 75,000 each. The apparent K m and V max 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. © 1994 Wiley‐Liss, Inc.