Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1984-11-2
pubmed:abstractText
Two anionic and two cationic glutathione-S-transferase (GST) isoenzymes were found in rat testes and purified to electrophoretic homogeneity. The enzymes are heterodimers with molecular weights of about 44 000 daltons and with widely overlapping specifities for electrophilic substrates. Only one isoenzyme yielded a positive immunoprecipitation reaction with antiserum against hepatic GST-B. The reactions with antiserum against hepatic GST-A were all negative. The Michaelis and association constants for some substrates were also determined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
599-607
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Purification and some properties of four glutathione-S-transferase isoenzymes from rat testes.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't