Meyer D J, Beale D, Tan K H, Coles B, Ketterer B
FEBS Lett. 1985 May 6;184(1):139-43. doi: 10.1016/0014-5793(85)80670-0.
A previously uncharacterized glutathione (GSH) transferase which is not apparent in normal liver, accounts for at least 25% of the soluble GSH transferase content of primary hepatomas induced by feeding N,N-dimethyl-4-aminoazobenzene. This enzyme is readily isolated, has an isoelectric point of 6.8, is composed of two identical subunits of apparent Mr 26000 and has GSH transferase activity towards a number of substrates including benzo(a)pyrene-7,8-diol-9,10-oxide. It is unusual in that it has GSH peroxidase activity towards fatty acid hydroperoxides but not towards the model substrates, cumene hydroperoxide and t-butyl hydroperoxide. It has been shown by tryptic peptide analysis to be distinct from GSH transferases composed of subunits 1, 2, 3, 4 or 6 and has been designated GSH transferase 7-7.
一种在正常肝脏中不明显的、以前未被鉴定的谷胱甘肽（GSH）转移酶，在喂食N，N-二甲基-4-氨基偶氮苯诱导的原发性肝癌中，占可溶性GSH转移酶含量的至少25%。这种酶很容易分离，其等电点为6.8，由两个表观分子量为26000的相同亚基组成，并且对包括苯并（a）芘-7，8-二醇-9，10-环氧化物在内的多种底物具有GSH转移酶活性。它不同寻常之处在于，它对脂肪酸氢过氧化物具有GSH过氧化物酶活性，但对模型底物氢过氧化异丙苯和叔丁基过氧化氢没有该活性。经胰蛋白酶肽分析表明，它与由亚基1、2、3、4或6组成的GSH转移酶不同，并被命名为GSH转移酶7-7。
