rdf:type |
|
lifeskim:mentions |
umls-concept:C0006556,
umls-concept:C0017262,
umls-concept:C0017837,
umls-concept:C0020792,
umls-concept:C0086418,
umls-concept:C0185117,
umls-concept:C0456387,
umls-concept:C0679058,
umls-concept:C1415330,
umls-concept:C1415331,
umls-concept:C1547699,
umls-concept:C2003941,
umls-concept:C2700640,
umls-concept:C2911684
|
pubmed:dateCreated |
1998-4-16
|
pubmed:databankReference |
|
pubmed:abstractText |
The Expressed Sequence Tag database has been searched for examples of previously undescribed human Alpha class glutathione transferases. An incomplete transcript of the previously described GSTA3 gene was identified in a cDNA library derived from 8-9 week placenta. This indicates that the GSTA3 gene is functional and is possibly under specific developmental regulation. A second cDNA, termed GSTA4, was identified in a brain cDNA library. The encoded GSTA4-4 enzyme was expressed in Escherichia coli and was found to be immunologically distinct from GSTA1-1 and to have high activity with alk-2-enals. Although GSTA4-4 appears to be functionally similar to the mouse GST5.7 and rat GST8-8 Alpha class enzymes, sequence comparisons and phylogenetic analysis suggest that GSTA4-4 may be a member of a distinct Alpha class subgroup.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-1329668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-1339283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-1427860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-1599415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-17248440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-2018473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-2345169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-2590177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-3031680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-3036131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-3196325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-3325043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-3447015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-3663118,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-3800996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-388439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-5114977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-6254573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-7159389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-7704666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-7904605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-7929235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-8074309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-8142470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-8198545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-8241281,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-8617493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-8617505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-8645150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-8770536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-8920976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-907137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480897-9396740
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0264-6021
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
330 ( Pt 2)
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
827-31
|
pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:9480897-Amino Acid Sequence,
pubmed-meshheading:9480897-Animals,
pubmed-meshheading:9480897-Base Sequence,
pubmed-meshheading:9480897-Brain,
pubmed-meshheading:9480897-Chickens,
pubmed-meshheading:9480897-DNA, Complementary,
pubmed-meshheading:9480897-Databases, Factual,
pubmed-meshheading:9480897-Gene Library,
pubmed-meshheading:9480897-Glutathione Transferase,
pubmed-meshheading:9480897-Humans,
pubmed-meshheading:9480897-Mice,
pubmed-meshheading:9480897-Molecular Sequence Data,
pubmed-meshheading:9480897-Rats,
pubmed-meshheading:9480897-Sequence Alignment,
pubmed-meshheading:9480897-Sequence Tagged Sites
|
pubmed:year |
1998
|
pubmed:articleTitle |
Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4.
|
pubmed:affiliation |
John Curtin School of Medical Research, Australian National University, GPO Box 334, Canberra ACT 2601, Australia.
|
pubmed:publicationType |
Journal Article,
Comparative Study
|