Glutathione transferases in primary rat hepatomas: the isolation of a form with GSH peroxidase activity
Glutathione transferases in primary rat hepatomas: the isolation of a form with GSH peroxidase activity
复制标题
原发性大鼠肝癌中的谷胱甘肽转移酶：具有 GSH 过氧化物酶活性的形式的分离
DOI：
10.1016/0014-5793(85)80670-0
复制
发表时间：
1985
期刊：
影响因子：
3.5
通讯作者：
B. Ketterer
中科院分区：
文献类型：
--
作者：
D. Meyer;Denis Beale;K. Tan;B. Coles;B. Ketterer
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 feedingN,N‐dimethyl‐4‐aminoazobenzene. This enzyme is readily isolated, has an isoelectric point of 6.8, is composed of two identical subunits of apparentMr26 000 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 andt‐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.
化学物质逐步发展癌症的细胞生物化学：G. H. A. Clowes 纪念讲座。
影响因子：
11.2
作者：
Farber,E
通讯作者：
Farber,E