Rhoads D M, Zarlengo R P, Tu C P
Biochem Biophys Res Commun. 1987 May 29;145(1):474-81. doi: 10.1016/0006-291x(87)91345-3.
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.
我们已经鉴定出了人肝脏谷胱甘肽S-转移酶Ha亚基的第二个cDNA序列pGTH2。除了其3'非编码序列较长外,它与Ha亚基1的cDNA pGTH1在碱基水平上有95%的同源性。我们的结果表明,多种碱性人肝脏谷胱甘肽S-转移酶是不同基因的产物。脱酰胺作用可能是产生谷胱甘肽S-转移酶同工酶多样性的一个生理重要过程的提议[神坂和夫、哈比格、W.H.、凯特利、J.N.、阿里亚斯、I.M.和雅各比、W.B.(1975年)《欧洲生物化学杂志》60,153 - 161]几乎可以被排除。