Purification of human hepatic glutathione S-transferases and the development of a radioimmunoassay for their measurement in plasma

J D Hayes, D Gilligan, B J Chapman, G J Beckett

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    Abstract

    A purification scheme is described for six human hepatic glutathione S-transferases from a single liver. Five of the transferases comprised Ya monomers and had a molecular mass of 44 000. The remaining enzyme comprised Yb monomers and had a molecular mass of 47 000. Data are presented demonstrating that there are at least two distinct Ya monomers. A radioimmunoassay has been developed that has sufficient precision and sensitivity to allow direct measurement of glutathione S-transferase concentrations in unextracted plasma. A comparison of aminotransferase and glutathione S-transferase levels, in three patients who had taken a paracetamol overdose, indicated that glutathione S-transferase measurements provided a far more sensitive index of hepatocellular integrity than the more conventional aminotransferase measurements.

    Original languageEnglish
    Pages (from-to)107-21
    Number of pages15
    JournalClinica Chimica Acta
    Volume134
    Issue number1-2
    Publication statusPublished - 31 Oct 1983

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    Keywords

    • Alanine Transaminase/blood
    • Aspartate Aminotransferases/blood
    • Chromatography, Affinity/methods
    • Cross Reactions
    • Glutathione Transferase/blood
    • Humans
    • Liver/enzymology
    • Male
    • Middle Aged
    • Molecular Weight
    • Radioimmunoassay/methods

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