Abstract
The occurrence of soluble glutathione S-transferase (GST) in the prostate of rat, guinea pig and rabbit is reported. With 1-chloro-2,4-dinitrobenzene (CDNB) as the second substrate a specific activity of 59 nmol product/min/mg protein was found in the rat. A value of approx. 2 x and 25 x higher was found for guinea-pig and rabbit respectively. GST activity was also demonstrated with 3 other substrates. GST C was the most abundant CDNB—GST isoenzyme (76%) in rat prostate, followed by GST A (17%) and GST AA (7%), significant amounts of other isoenzymes not being found. The presence of GST in the prostate suggests that these enzymes may play a role in the metabolism and detoxification of electrophilic xenobiotics.
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