Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1995-1-5
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1040-452X
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
404-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Purification and characterization of beta-glucuronidase from bull seminal plasma and its role in fertilization.
pubmed:affiliation
Department of Biochemistry, University of Georgia, Athens 30602.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.