| Literature DB >> 3036131 |
D M Rhoads, R P Zarlengo, C P Tu.
Abstract
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.Entities:
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Year: 1987 PMID: 3036131 DOI: 10.1016/0006-291x(87)91345-3
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575