Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-12-22
pubmed:databankReference
pubmed:abstractText
A full-length cDNA clone encoding the previously purified mouse glutathione S-transferase GST 5.7 [(1991), Biochem. J. 278, 793-799] has been isolated from a mouse lung cDNA library in lambda gt11. Sequencing of the clone revealed the presence of microheterogeneity in GST 5.7. Comparison of the deduced protein sequence with other glutathione S-transferases, together with previous information available on GST 5.7, indicates that the enzyme belongs to a novel subgroup within the alpha class of glutathione S-transferases. Members of the subgroup, which also include the rat GST 8-8 and perhaps chicken GST CL3, show high sequence homology with each other, but only moderate similarity to other alpha class enzymes. They share a substrate specificity profile that resembles pi-class enzymes, and are active in the conjugation of lipid peroxidation products.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
313
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
A subgroup of class alpha glutathione S-transferases. Cloning of cDNA for mouse lung glutathione S-transferase GST 5.7.
pubmed:affiliation
Department of Medicine, University of Arkansas for Medical Sciences, Little Rock 72205.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.