Human microsomal glutathione S-transferase: Its involvement in the conjugation of hexachlorobuta-1,3-diene with glutathione

L I McLellan, C R Wolf, J D Hayes

    Research output: Contribution to journalArticle

    53 Citations (Scopus)

    Abstract

    A microsomal glutathione S-transferase (GST) was purified from human liver. This enzyme was shown to have characteristics similar to those of the rat microsomal GST described by Morgenstern & De Pierre [(1983) Eur. J. Biochem. 134, 591-597]. The specific activity of human microsomal GST towards 1-chloro-2,4-dinitrobenzene or cumene hydroperoxide can be stimulated by treating the enzyme with N-ethylmaleimide. This enhancement of activity is accompanied by increased sensitivity to inhibition by haematin and cholic acid. The subunit Mr values of the rat and human enzymes are similar (approx. 17,300), and the proteins are immunologically related. During purification, both human and rat microsomal GST enzymes are the only hepatic proteins obtained from Triton X-100-solubilized microsomal fractions that show activity towards the nephrotoxin hexachlorobuta-1,3-diene. The involvement of microsomal GST in toxification reactions is discussed.

    Original languageEnglish
    Pages (from-to)87-93
    Number of pages7
    JournalBiochemical Journal
    Volume258
    Issue number1
    Publication statusPublished - 15 Feb 1989

    Fingerprint

    Glutathione Transferase
    Glutathione
    Enzymes
    Rats
    Cholic Acid
    Hemin
    Ethylmaleimide
    Liver
    Octoxynol
    Dinitrochlorobenzene
    Human Activities
    Proteins
    Purification
    hexachlorobutadiene

    Keywords

    • Animals
    • Butadienes/metabolism
    • Catalysis
    • Glutathione/metabolism
    • Glutathione Transferase/isolation & purification
    • Humans
    • Ligands/metabolism
    • Male
    • Microsomes, Liver/enzymology
    • Rats
    • Rats, Inbred Strains

    Cite this

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    title = "Human microsomal glutathione S-transferase: Its involvement in the conjugation of hexachlorobuta-1,3-diene with glutathione",
    abstract = "A microsomal glutathione S-transferase (GST) was purified from human liver. This enzyme was shown to have characteristics similar to those of the rat microsomal GST described by Morgenstern & De Pierre [(1983) Eur. J. Biochem. 134, 591-597]. The specific activity of human microsomal GST towards 1-chloro-2,4-dinitrobenzene or cumene hydroperoxide can be stimulated by treating the enzyme with N-ethylmaleimide. This enhancement of activity is accompanied by increased sensitivity to inhibition by haematin and cholic acid. The subunit Mr values of the rat and human enzymes are similar (approx. 17,300), and the proteins are immunologically related. During purification, both human and rat microsomal GST enzymes are the only hepatic proteins obtained from Triton X-100-solubilized microsomal fractions that show activity towards the nephrotoxin hexachlorobuta-1,3-diene. The involvement of microsomal GST in toxification reactions is discussed.",
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    year = "1989",
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    language = "English",
    volume = "258",
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    journal = "Biochemical Journal",
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    Human microsomal glutathione S-transferase : Its involvement in the conjugation of hexachlorobuta-1,3-diene with glutathione. / McLellan, L I; Wolf, C R; Hayes, J D.

    In: Biochemical Journal, Vol. 258, No. 1, 15.02.1989, p. 87-93.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Human microsomal glutathione S-transferase

    T2 - Its involvement in the conjugation of hexachlorobuta-1,3-diene with glutathione

    AU - McLellan, L I

    AU - Wolf, C R

    AU - Hayes, J D

    PY - 1989/2/15

    Y1 - 1989/2/15

    N2 - A microsomal glutathione S-transferase (GST) was purified from human liver. This enzyme was shown to have characteristics similar to those of the rat microsomal GST described by Morgenstern & De Pierre [(1983) Eur. J. Biochem. 134, 591-597]. The specific activity of human microsomal GST towards 1-chloro-2,4-dinitrobenzene or cumene hydroperoxide can be stimulated by treating the enzyme with N-ethylmaleimide. This enhancement of activity is accompanied by increased sensitivity to inhibition by haematin and cholic acid. The subunit Mr values of the rat and human enzymes are similar (approx. 17,300), and the proteins are immunologically related. During purification, both human and rat microsomal GST enzymes are the only hepatic proteins obtained from Triton X-100-solubilized microsomal fractions that show activity towards the nephrotoxin hexachlorobuta-1,3-diene. The involvement of microsomal GST in toxification reactions is discussed.

    AB - A microsomal glutathione S-transferase (GST) was purified from human liver. This enzyme was shown to have characteristics similar to those of the rat microsomal GST described by Morgenstern & De Pierre [(1983) Eur. J. Biochem. 134, 591-597]. The specific activity of human microsomal GST towards 1-chloro-2,4-dinitrobenzene or cumene hydroperoxide can be stimulated by treating the enzyme with N-ethylmaleimide. This enhancement of activity is accompanied by increased sensitivity to inhibition by haematin and cholic acid. The subunit Mr values of the rat and human enzymes are similar (approx. 17,300), and the proteins are immunologically related. During purification, both human and rat microsomal GST enzymes are the only hepatic proteins obtained from Triton X-100-solubilized microsomal fractions that show activity towards the nephrotoxin hexachlorobuta-1,3-diene. The involvement of microsomal GST in toxification reactions is discussed.

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    KW - Catalysis

    KW - Glutathione/metabolism

    KW - Glutathione Transferase/isolation & purification

    KW - Humans

    KW - Ligands/metabolism

    KW - Male

    KW - Microsomes, Liver/enzymology

    KW - Rats

    KW - Rats, Inbred Strains

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    M3 - Article

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