Source:http://linkedlifedata.com/resource/pubmed/id/10209291
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1999-6-1
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pubmed:abstractText |
The major form of glutathione transferase from the toad liver previously designed as Bufo bufo liver GST-7.6 (A. Aceto, B. Dragani, T. Bucciarelli, P. Sacchetta, F. Martini, S. Angelucci, F. Amicarelli, M. Miranda and C. Di Ilio, Biochem. J. 289 (1993) 417-422) has been characterized. According to its partial amino acid sequence, the toad enzyme may be included in the pi class GST and named bbGST P2-2. However, bbGST P2-2 appears to be immunologically, structurally and kinetically distinct from any other members of pi family, including bbGST P1-1, suggesting that it may constitute a subset of pi class GST. The data support the hypothesis that the transition from aquatic to terrestrial life causes a switch of the GST amphibian pattern promoting the expression of a GST form (bbGST P2-2) able to counteract, with higher efficiency, the toxic effects of reactive metabolites of oxidative metabolism and those of hydrophobic xenobiotics.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
1431
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
189-98
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10209291-Amino Acid Sequence,
pubmed-meshheading:10209291-Amphibians,
pubmed-meshheading:10209291-Animals,
pubmed-meshheading:10209291-Bufo bufo,
pubmed-meshheading:10209291-Glutathione Transferase,
pubmed-meshheading:10209291-Hydrogen-Ion Concentration,
pubmed-meshheading:10209291-Kinetics,
pubmed-meshheading:10209291-Liver,
pubmed-meshheading:10209291-Molecular Sequence Data,
pubmed-meshheading:10209291-Sulfhydryl Reagents,
pubmed-meshheading:10209291-Temperature
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pubmed:year |
1999
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pubmed:articleTitle |
Characterization of toad liver glutathione transferase.
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pubmed:affiliation |
Dipartimento di Scienze Biomediche, Università 'G. D'Annunzio', 66100, Chieti, Italy.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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