Linked Life Data

4065244

Source:http://linkedlifedata.com/resource/pubmed/id/4065244

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-12-24
pubmed:abstractText
Human lens has two forms of glutathione S-transferase having pI values of greater than 10 and 4.4. Both of these enzymes may have been purified to an apparent homogeneity from normal human lenses using glutathione affinity chromatography and isoelectric focusing. These two isoenzymes are significantly different from each other in their kinetic, structural, and immunological properties. The cationic form (pI greater than 10) is a dimer of Mr 24 500 subunits whereas the anionic form (pI 4.4) is a dimer of Mr 22 500 subunits. Neither of the two forms express selenium-independent glutathione peroxidase II activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-4835
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
201-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Purification and characterization of the two forms of glutathione S-transferase present in human lens.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.