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Activation and inhibition of microsomal glutathione transferase from mouse liver.
Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden.
Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden.ORCID iD: 0000-0003-3927-4394
Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden.
1988 (English)In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 249, no 3, 819-23 p.Article in journal (Refereed) Published
Abstract [en]

Mouse liver microsomal glutathione transferase was purified in an N-ethylmaleimide-activated as well as an unactivated form. The enzyme had a molecular mass of 17 kDa and a pI of 8.8. It showed cross-reactivity with antibodies raised against rat liver microsomal glutathione transferase, but not with any of the available antisera raised against cytosolic glutathione transferases. The fully N-ethylmaleimide-activated enzyme could be further activated 1.5-fold by inclusion of 1 microM-bromosulphophthalein in the assay system. The latter effect was reversible, which was not the case for the N-ethylmaleimide activation. At 20 microM-bromosulphophthalein the activated microsomal glutathione transferase was strongly inhibited, while the unactivated form was activated 2.5-fold. Inhibitors of the microsomal glutathione transferase from mouse liver showed either about the same I50 values for the activated and the unactivated form of the enzyme, or significantly lower I50 values for the activated form compared with the unactivated form. The low I50 values and the steep slope of the activity-versus-inhibitor-concentration curves for the latter group of inhibitors tested on the activated enzyme indicate a co-operative effect involving conversion of activated enzyme into the unactivated form, as well as conventional inhibition of the enzyme.

Place, publisher, year, edition, pages
1988. Vol. 249, no 3, 819-23 p.
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Medical and Health Sciences
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URN: urn:nbn:se:liu:diva-99872ISI: A1988M048900028PubMedID: 3355500OAI: oai:DiVA.org:liu-99872DiVA: diva2:658706
Available from: 2013-10-22 Created: 2013-10-22 Last updated: 2017-12-06

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