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A new glutathione S-transferase has been purified to homogeneity from 105,000 X g supernatant of Sprague-Dawley rat liver homogenates. The purified enzyme exhibited specific activities of approximately 1.8, and 0.12 mumoles X min-1 X 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 (Y alpha Family). Our in vitro 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 S-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 mumoles. min-1 X mg-1 respectively.
C C Reddy, and
N Li, and
C P Tu
January 1985,
Methods in enzymology,
C C Reddy, and
N Li, and
C P Tu
April 1984,
Nihon Shokakibyo Gakkai zasshi = The Japanese journal of gastro-enterology,
C C Reddy, and
N Li, and
C P Tu
October 1985,
Archives of biochemistry and biophysics,
C C Reddy, and
N Li, and
C P Tu
March 1983,
Biochemical and biophysical research communications,
C C Reddy, and
N Li, and
C P Tu
December 1983,
The Biochemical journal,
C C Reddy, and
N Li, and
C P Tu
November 1988,
Biochemistry international,
C C Reddy, and
N Li, and
C P Tu
June 1986,
The Journal of biological chemistry,
C C Reddy, and
N Li, and
C P Tu
August 1976,
Archives of biochemistry and biophysics,
C C Reddy, and
N Li, and
C P Tu
January 1980,
Acta chemica Scandinavica. Series B: Organic chemistry and biochemistry,
C C Reddy, and
N Li, and
C P Tu
May 2000,
Archives of toxicology,
