Singhal S S, Zimniak P, Awasthi S, Piper J T, He N G, Teng J I, Petersen D R, Awasthi Y C
Department of Internal Medicine, University of Texas Medical Branch, Galveston 77555.
Arch Biochem Biophys. 1994 Jun;311(2):242-50. doi: 10.1006/abbi.1994.1233.
A human acidic glutathione S-transferase, hGST 5.8, was isolated from heart, pancreas, and brain by a procedure involving immunoadsorption chromatography on immobilized antibodies raised against mouse mGSTA4-4. The human hGST 5.8 enzymes isolated from these tissues had similar pI (5.8) and subunit M(r) (24.5 kDa) values, showed about 17- to 20-fold higher specific activities for 4-hydroxynon-2-enal than that for 1-chloro-2,4-dinitrobenzene, and expressed glutathione peroxidase activity toward phospholipid hydroperoxides. In this respect, the enzymes belong together with rat GST 8-8 and mouse mGSTA4-4 to a subgroup of GSTs involved in the detoxification of lipid peroxidation products. Partial sequencing of CNBr-peptide fragments of hGST 5.8 proteins isolated from various human tissues revealed significant similarity to mGSTA4-4 and the existence of several distinct isoforms differing in their primary structures. These isoforms had similar but nevertheless clearly distinguishable catalytic properties. These results indicate the existence of multiple hGST 5.8-related genes in the humans, which is consistent with our previous studies showing the presence of several closely related genes for the mouse ortholog mGSTA4-4 (Zimniak et al., J. Biol. Chem., 1994, 269, 992-1000).
通过一种程序从心脏、胰腺和大脑中分离出一种人类酸性谷胱甘肽S-转移酶hGST 5.8，该程序包括在针对小鼠mGSTA4-4产生的固定化抗体上进行免疫吸附色谱。从这些组织中分离出的人类hGST 5.8酶具有相似的pI（5.8）和亚基M(r)（24.5 kDa）值，对4-羟基壬-2-烯醛的比活性比对1-氯-2,4-二硝基苯高约17至20倍，并对磷脂氢过氧化物表现出谷胱甘肽过氧化物酶活性。在这方面，这些酶与大鼠GST 8-8和小鼠mGSTA4-4属于参与脂质过氧化产物解毒的谷胱甘肽S-转移酶亚组。对从各种人类组织中分离出的hGST 5.8蛋白的CNBr肽片段进行部分测序，发现与mGSTA4-4有显著相似性，并且存在几种一级结构不同的明显异构体。这些异构体具有相似但仍明显可区分的催化特性。这些结果表明人类中存在多个与hGST 5.8相关的基因，这与我们之前的研究一致，之前的研究表明小鼠直系同源物mGSTA4-4存在几个密切相关的基因（齐米亚克等人，《生物化学杂志》，1994年，269卷，992 - 1000页）。
