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. 1991 Mar 1;274(Pt 2):405–408. doi: 10.1042/bj2740405

Purification and characterization of acidic glutathione S-transferase 6 from human brain.

T Suzuki 1, D C Shaw 1, P G Board 1
PMCID: PMC1150152  PMID: 2006908

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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