The basic glutathione S-transferases from human livers are products of separate genes.
We have characterized a second cDNA sequence, pGTH2, for the human liver glutathione S-transferases Ha subunits. It is 95% homologous base-for-base to the Ha subunit 1 cDNA, pGTH1, except for its longer 3' noncoding sequences. Our results indicate that the multiple basic human liver glutathione S-transferases are products of separate genes. The proposal [Kamisaka, K., Habig, W. H., Ketley, J. N., Arias, I. M., and Jakoby, W. B. (1975) Eur. J. Biochem. 60, 153-161] that deamidation may be a physiologically important process for generating glutathione S-transferases isozyme multiplicity can be all but ruled out.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000032:analysis; D004262:DNA Restriction Enzymes; D005796:Genes; D005982:Glutathione Transferase / Q000235:genetics*; D006801:Humans; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D010944:Plants / Q000201:enzymology; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D003313:Zea mays / Q000201:enzymology
D046911:Macromolecular Substances; D004247:DNA; D005982:Glutathione Transferase; D004262:DNA Restriction Enzymes