Linked Life Data

7371010

Source:http://linkedlifedata.com/resource/pubmed/id/7371010

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1980-7-26
pubmed:abstractText
Glutathione S-transferases have been purified to homogeneity from Chinese hamster liver. Three enzyme forms were separated and designated Forms I, II, and III in order of their elution from carboxymethylcellulose columns. The forms exhibit close physical similarities to glutathione S-transferases B (ligandin) of rat liver and epsilon of humam liver. However, enzyme kinetic analysis indicates that the hamster enzymes exhibit similar Km values but higher Vmax values towards common substrates compared with the rat and human forms. These differences, which explain the increased enzymic activities of hamster glutathione S-transferases in vivo and in vitro, appear to be related to slight differences in the peptide composition of hamster liver glutathione S-transferases compared to the rat and human enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1787-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Purification and properties of hamster liver ligandins, glutathione S-transferases.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.