Document Detail


Purification and characterization of acidic glutathione S-transferase 6 from human brain.
MedLine Citation:
PMID:  2006908     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
T Suzuki; D C Shaw; P G Board
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  274 ( Pt 2)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1991 Mar 
Date Detail:
Created Date:  1991-04-22     Completed Date:  1991-04-22     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  405-8     Citation Subset:  IM    
Affiliation:
Human Genetics Group, John Curtin School of Medical Research, Australian National University, Canberra.
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MeSH Terms
Descriptor/Qualifier:
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:
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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