Linked Life Data

1503563

Source:http://linkedlifedata.com/resource/pubmed/id/1503563

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-9-16
pubmed:abstractText
Glutathione S-transferase has been purified from bovine erythrocytes by affinity chromatography. The enzyme has an isoelectric point of 7.2, behaves as a 48-kDa protein composed of two identical subunits, and has an N-terminal sequence of PPYTIVYFPVQGR?EAMRMLL. This sequence, the amino acid composition, and the kinetic parameters suggest that the enzyme belongs to the pi-class of transferases. Hemins, porphyrins, and fatty acids form complexes with the enzyme and serve as effective inhibitors. Treatment of the transferase with N-ethylmaleimide, 3-amino-1,2,4-triazole, diethyl pyrocarbonate, or 2,3-butanedione inhibits transferase activity without altering tetrapyrrole binding. The role of the complexation and inhibition of glutathione S-transferase in erythroid metabolism has yet to be elucidated.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
265-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Bovine erythrocyte glutathione S-transferase: purification, inhibition, and complex formation.
pubmed:affiliation
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-0606.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't