Glutathione transferases in primary rat hepatomas: the isolation of a form with GSH peroxidase activity

FEBS Letters

Ketterer, Brian¹  Meyer, David J.¹  Beale, Denis²  Coles, Brian¹  Tan, K.Hong¹ 

[1] Courtauld Institute of Biochemistry, Middlesex Hospital Medical School, London W1P 7PN, England;Agricultural Research Council Institute of Animal Physiology, Babraham, Cambridge, England

关键词: GSH transferase 7-7;    GSH peroxidase;    Hepatoma;    Purification;   

DOI  :  10.1016/0014-5793(85)80670-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 M _r 26 000 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 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.

【 授权许可】

Unknown