SEX DIFFERENCE IN SUBUNIT COMPOSITION OF HEPATIC GLUTATHIONE S-TRANSFERASE IN RATS
SEX DIFFERENCE IN SUBUNIT COMPOSITION OF HEPATIC GLUTATHIONE S-TRANSFERASE IN RATS
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DOI:
10.1093/oxfordjournals.jbchem.a135249
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发表时间:
1985-01-01
影响因子:
2.7
通讯作者:
KITAGAWA, H
中科院分区:
文献类型:
--
作者:
IGARASHI, T;SATOH, T;KITAGAWA, H
The activities of hepatic cytosolic glutathione S-transferases (GST) towards 1,2-dichloro-4-nitrobenzene in male rats were higher than those in females. The enzyme activities towards 1-chloro-2,4-dinitrobenzene were not significantly different between the 2 sexes. SDS-PAGE [sodium dodecyl sulfate-polyacrylamide gel electrophoresis] analysis of GST purified from male and female rat hepatic cytosols by affinity column chromatography showed that there was a significant difference in the subunit composition between the 2 sexes. With regard to the several isozymes of GST in male and female rats, isozymes with basic and neutral/acidic isoelectric points were separated into 7 molecular species by chromatofocusing. The sex differences in the quantitative proportions of GST isozymes were also confirmed by immunotitration using anti-GST-BL and -AC antibodies. Glutathione peroxidase (GSH-Px) activities in rat hepatic cytosol towards hydrogen peroxide and cumene hydroperoxide were markedly higher in females than in males. Of the 2 types of GSH-Px, selenoenzyme (Se-GSH-Px) and the Se-independent enzyme (non-Se-GSH-Px), the former was mainly responsible for the sex difference in the enzyme activities. The GSH-Px activity of GST, non-Se-GSH-Px, was also higher in females than that in males. Since GST isozymes of the BL type possess GSH-Px activity towards cumene hydroperoxide, the increased activities of non-Se-GSH-Px in the female hepatic cytosol seemed to be mainly due to the increased transferase activities of the isozymes, GST-L2 and -BL.