Linked Life Data

3905421

Source:http://linkedlifedata.com/resource/pubmed/id/3905421

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1985-12-27
pubmed:abstractText
Two cationic (pIs 9.1 and 7.6) and one anionic (pI 4.4) forms of glutathione S-transferase have been purified to an apparent homogeneity from human cornea using glutathione-linked affinity chromatography and isoelectric focusing. The substrate specificities of the three enzyme forms are significantly different from each other. None of the three forms of human cornea glutathione S-transferase express glutathione peroxidase II activity. Immunological and structural studies reveal that human cornea enzymes have structural similarities with glutathione S-transferases of other human tissues.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-4835
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
431-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Characterization of glutathione S-transferases of human cornea.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.