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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May 1987
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Research Article|
May 15 1987
Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver
P K Stockman;
P K Stockman
1University of Edinburgh Department of Clinical Chemistry, Royal Infirmary, Scotland, U.K.
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L I McLellan;
L I McLellan
1University of Edinburgh Department of Clinical Chemistry, Royal Infirmary, Scotland, U.K.
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J D Hayes
J D Hayes
1University of Edinburgh Department of Clinical Chemistry, Royal Infirmary, Scotland, U.K.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1987 London: The Biochemical Society
1987
Biochem J (1987) 244 (1): 55–61.
Citation
P K Stockman, L I McLellan, J D Hayes; Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver. Biochem J 15 May 1987; 244 (1): 55–61. doi: https://doi.org/10.1042/bj2440055
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