| Purification and characterization of acidic glutathione S-transferase 6 from human brain. | |
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MedLine Citation:
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PMID: 2006908 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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An acidic glutathione S-transferase (GST) isoenzyme termed GST6 has been isolated from human brain, characterized and compared with other isoenzymes. The N-terminal amino acid sequence of GST6 was found to be identical with that of GST4 previously purified from human muscle. GST6 cross-reacted with antibody raised against GST4, but not with antisera raised against GST1, GST2 or GST3. The subunit Mr and pI of GST6 were found to be different from those of GST4. The present results indicate that GST6 is another member of the Mu evolutionary class which in man also includes GST1, GST4 and GST5. A minor component that co-purified with GST6 was shown to have an N-terminal sequence similar to, but not identical with, that of GST3. This isoenzyme may be an additional member of the Pi evolutionary class. |
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Authors:
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T Suzuki; D C Shaw; P G Board |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Biochemical journal Volume: 274 ( Pt 2) ISSN: 0264-6021 ISO Abbreviation: Biochem. J. Publication Date: 1991 Mar |
Date Detail:
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Created Date: 1991-04-22 Completed Date: 1991-04-22 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 405-8 Citation Subset: IM |
Affiliation:
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Human Genetics Group, John Curtin School of Medical Research, Australian National University, Canberra. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adult Amino Acid Sequence Brain / enzymology* Chromatography, Affinity Chromatography, DEAE-Cellulose Glutathione Transferase / genetics, isolation & purification*, metabolism Humans Hydrogen-Ion Concentration Isoenzymes / genetics, isolation & purification*, metabolism Kinetics Male Molecular Sequence Data Sequence Homology, Nucleic Acid |
| Chemical | |
Reg. No./Substance:
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0/Isoenzymes; EC 2.5.1.18/Glutathione Transferase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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