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. 1987 Apr;84(8):2377–2381. doi: 10.1073/pnas.84.8.2377

Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12.

P G Board, G C Webb
PMCID: PMC304654  PMID: 3031680

Abstract

The glutathione S-transferases (GST) (glutathione transferase; EC 2.5.1.18) are a family of enzymes responsible for the metabolism of a broad range of xenobiotics and carcinogens. A cDNA clone containing the entire amino acid coding sequence of a human GST-2 subunit has been isolated using a lambda gt11 expression library. The complete nucleotide sequence and a partial restriction map are presented. The subunit is composed of 221 amino acids with a molecular weight of 25,425 before posttranslational modification. The deduced amino acid sequence is rich in lysine, which is consistent with the relatively high pI of GST-2. The human sequence shows considerable homology with the rat Ya and Yc GST sequences but little homology with the rat GSTp and Yb subunit sequences. Southern blots of restriction digests of human DNA indicate that there may be multiple GST-2 genes. In situ hybridization of the cloned cDNA to human chromosomes produces intense labeling only over band p12 on the short arm of chromosome 6 near the centromere. This indicates that the GST-2 gene(s) are located only at this site.

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Selected References

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