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Di Simplicio P, Jensson H, Mannervik B. Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase. Biochem J. 1989;263(3):679-85doi: 10.1042/bj2630679.
Di Simplicio, P., Jensson, H., & Mannervik, B. (1989). Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase. The Biochemical journal, 263(3), 679-85. https://doi.org/10.1042/bj2630679
Di Simplicio, P, et al. "Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase." The Biochemical journal vol. 263,3 (1989): 679-85. doi: https://doi.org/10.1042/bj2630679
Di Simplicio P, Jensson H, Mannervik B. Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase. Biochem J. 1989 Nov 01;263(3):679-85. doi: 10.1042/bj2630679. PMID: 2597126; PMCID: PMC1133486.
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Biochem J. 1989 Nov 01;263(3):679-85. doi: 10.1042/bj2630679.

Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase.

The Biochemical journal

P Di Simplicio, H Jensson, B Mannervik

Affiliations

  1. Department of Environmental Biology, University of Siena, Italy.

PMID: 2597126 PMCID: PMC1133486 DOI: 10.1042/bj2630679
Free PMC Article

Abstract

The cytosolic glutathione transferases (GSTs) with basic pI values have been studied in mouse liver after treatment with 2,3-t-butylhydroxyanisole (BHA), cafestol palmitate (CAF), phenobarbital (PB), 3-methylcholanthrene (3-MC) and trans-stilbene oxide (t-SBO). The cytosolic GST activity was induced by all compounds except for 3-MC. Three forms of GST were isolated by means of affinity chromatography and f.p.l.c. The examination of protein profiles and enzymic activities with specific substrates showed that the three GSTs correspond to those found in control animals, i.e. GSTs MI, MII and MIII. The class Mu GST MIII accounted for the major effect of induction, whereas the class Alpha GST MI and the class Pi GST MII were unchanged or somewhat down-regulated. The greatest induction was obtained with BHA, PB and CAF. The activities of other glutathione-dependent enzymes were also studied. An increase in glutathione reductase and thioltransferase activities was observed after BHA, PB or CAF treatment; glyoxalase I and Se-dependent glutathione peroxidase were depressed in comparison with the control group in all cases studied.

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