A purification scheme is described for a glutathione S-transferase (GST) from human liver that catalyses the conjugation of 1-menaphthyl sulphate (MS) with GSH; the method devised results in an approx. 500-fold increase in specific activity towards MS. The human enzyme which metabolizes MS is a homodimer comprising subunits of M(r) 25,100, and immunochemical experiments have shown it to be a member of the class-Theta GSTs. Automated Edman degradation of this enzyme has confirmed that it is a Theta-class GST bu the amino acid sequence obtained differs from that of GST theta described previously [Meyer, Coles, Pemble, Gilmore, Fraser & Ketterer (1991) Biochem. J. 274, 409-414]. We have therefore designated the enzyme that catalyses the conjugation of MS with GSH GST T2-2* (in the absence of complete amino acid sequence data, the T1 and T2 subunits are provisionally designated T1* and T2*); the evidence which indicates that GST theta (which should possibly now be called GST T1-1*) and GST T2-2* represent distinct isoenzymes is discussed.
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Research Article|
September 15 1992
Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate
A J Hussey;
A J Hussey
1University Department of Clinical Biochemistry, The Royal Infirmary, Edinburgh EH3 9YW, Scotland, U.K.
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J D Hayes
J D Hayes
1University Department of Clinical Biochemistry, The Royal Infirmary, Edinburgh EH3 9YW, Scotland, U.K.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1992 The Biochemical Society, London
1992
Biochem J (1992) 286 (3): 929–935.
Citation
A J Hussey, J D Hayes; Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate. Biochem J 15 September 1992; 286 (3): 929–935. doi: https://doi.org/10.1042/bj2860929
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