Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate

A J Hussey, J D Hayes

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    76 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)929-35
    Number of pages7
    JournalBiochemical Journal
    Volume286 ( Pt 3)
    DOIs
    Publication statusPublished - 15 Sep 1992

    Keywords

    • Amino Acid Sequence
    • Blotting, Western
    • Chromatography, High Pressure Liquid
    • Cytosol/enzymology
    • Electrophoresis, Polyacrylamide Gel
    • Glutathione Transferase/chemistry
    • Humans
    • Immunochemistry
    • Liver/enzymology
    • Molecular Sequence Data
    • Naphthalenes/metabolism
    • Peptide Mapping
    • Sequence Homology, Nucleic Acid

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