Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver

P K Stockman, L I McLellan, J D Hayes

    Research output: Contribution to journalArticle

    44 Citations (Scopus)

    Abstract

    The basic glutathione S-transferases in human liver are composed of at least two immunochemically distinct polypeptides, designated B1 and B2. These subunits exist as homodimers, but can hybridize to form the B1B2 heterodimer [Stockman, Beckett & Hayes (1985) Biochem. J. 227, 457-465]. Although these basic glutathione S-transferases possess similar catalytic properties, the B2 subunit exhibits significantly greater selenium-independent glutathione peroxidase activity than subunit B1. The use of the ligands haematin, tributyltin acetate and Bromosulphophthalein as inhibitors of 1-chloro-2,4-dinitrobenzene-GSH-conjugating activity clearly discriminate between the B1 and B2 subunits and should help facilitate their identification. Peptide mapping experiments showed that B1 and B2 are structurally distinct, but related, subunits; subunit B1 yielded 43 tryptic peptides, seven of which were unique, whereas subunit B2 yielded 40 tryptic peptides, four of which were unique.

    Original languageEnglish
    Pages (from-to)55-61
    Number of pages7
    JournalBiochemical Journal
    Volume244
    Issue number1
    Publication statusPublished - 15 May 1987

    Fingerprint

    Glutathione Transferase
    Liver
    Peptides
    Dinitrochlorobenzene
    Hemin
    Peptide Mapping
    Ligands
    Experiments

    Keywords

    • Amino Acids/analysis
    • Electrophoresis, Polyacrylamide Gel
    • Glutathione Transferase/antagonists & inhibitors
    • Humans
    • Isoenzymes/isolation & purification
    • Liver/enzymology
    • Peptide Mapping
    • Substrate Specificity

    Cite this

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    title = "Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver",
    abstract = "The basic glutathione S-transferases in human liver are composed of at least two immunochemically distinct polypeptides, designated B1 and B2. These subunits exist as homodimers, but can hybridize to form the B1B2 heterodimer [Stockman, Beckett & Hayes (1985) Biochem. J. 227, 457-465]. Although these basic glutathione S-transferases possess similar catalytic properties, the B2 subunit exhibits significantly greater selenium-independent glutathione peroxidase activity than subunit B1. The use of the ligands haematin, tributyltin acetate and Bromosulphophthalein as inhibitors of 1-chloro-2,4-dinitrobenzene-GSH-conjugating activity clearly discriminate between the B1 and B2 subunits and should help facilitate their identification. Peptide mapping experiments showed that B1 and B2 are structurally distinct, but related, subunits; subunit B1 yielded 43 tryptic peptides, seven of which were unique, whereas subunit B2 yielded 40 tryptic peptides, four of which were unique.",
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    year = "1987",
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    Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver. / Stockman, P K; McLellan, L I; Hayes, J D.

    In: Biochemical Journal, Vol. 244, No. 1, 15.05.1987, p. 55-61.

    Research output: Contribution to journalArticle

    TY - JOUR

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    AU - McLellan, L I

    AU - Hayes, J D

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    N2 - The basic glutathione S-transferases in human liver are composed of at least two immunochemically distinct polypeptides, designated B1 and B2. These subunits exist as homodimers, but can hybridize to form the B1B2 heterodimer [Stockman, Beckett & Hayes (1985) Biochem. J. 227, 457-465]. Although these basic glutathione S-transferases possess similar catalytic properties, the B2 subunit exhibits significantly greater selenium-independent glutathione peroxidase activity than subunit B1. The use of the ligands haematin, tributyltin acetate and Bromosulphophthalein as inhibitors of 1-chloro-2,4-dinitrobenzene-GSH-conjugating activity clearly discriminate between the B1 and B2 subunits and should help facilitate their identification. Peptide mapping experiments showed that B1 and B2 are structurally distinct, but related, subunits; subunit B1 yielded 43 tryptic peptides, seven of which were unique, whereas subunit B2 yielded 40 tryptic peptides, four of which were unique.

    AB - The basic glutathione S-transferases in human liver are composed of at least two immunochemically distinct polypeptides, designated B1 and B2. These subunits exist as homodimers, but can hybridize to form the B1B2 heterodimer [Stockman, Beckett & Hayes (1985) Biochem. J. 227, 457-465]. Although these basic glutathione S-transferases possess similar catalytic properties, the B2 subunit exhibits significantly greater selenium-independent glutathione peroxidase activity than subunit B1. The use of the ligands haematin, tributyltin acetate and Bromosulphophthalein as inhibitors of 1-chloro-2,4-dinitrobenzene-GSH-conjugating activity clearly discriminate between the B1 and B2 subunits and should help facilitate their identification. Peptide mapping experiments showed that B1 and B2 are structurally distinct, but related, subunits; subunit B1 yielded 43 tryptic peptides, seven of which were unique, whereas subunit B2 yielded 40 tryptic peptides, four of which were unique.

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    KW - Isoenzymes/isolation & purification

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    KW - Peptide Mapping

    KW - Substrate Specificity

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