Identification of a new glutathione -transferase from rat liver cytosol |
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Authors: | C.Channa Reddy Nan-qian Li Chen-Pei D. Tu |
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Affiliation: | 1. Department of Veterinary Science, Center for Air Environment Studies The Pennsylvania State University University Park, PA 16802 USA;2. Department of Biochemistry, Microbiology, Molecular & Cell Biology The Pennsylvania State University University Park, PA 16802 USA |
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Abstract: | A new glutathione -transferase has been purified to homogeneity from 105,000 × g supernatant of Sprague-Dawley rat liver homogenates. The purified enzyme exhibited specific activities of approximately 1.8, and 0.12 μmoles. min?1. mg?1 toward 1-chloro 2,4-dinitrobenzene and cumene hydroperoxide respectively. The SDS gel electrophoresis data on subunit composition revealed that the new transferase is composed of two subunits with an identical Mr of 24,400 (Yα Family). Our translation experiments with rat liver poly(A) RNAs and substrate specificity data suggest that this subunit is different from the previously reported Ya, Yb and Yc subunits of rat liver glutathione -transferases. Comparatively, the new isozyme showed significant activity toward 1,2 epoxy-3-(P-nitrophenoxy)-propane, ethacrynic acid and P-nitrophenyl acetate, 0.4, 0.34 and 0.18 μ moles. min?1. mg?1 respectively. |
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Keywords: | To whom correspondence should be addressed. |
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