The chemistry of the inhibition of blood xanthine oxidase by -SH reagents.
In this study it was shown that the rat blood serum xanthine oxidase (X.O.) is differently inhibited by -SH reagents and seems that the blood serum enzyme has two types of -SH groups, one reacting relatively rapidly and unrelated to the enzyme activity and the other reacting slowly to produce inactivation. The results presented suggest that there are only few fundamental relationship between the different -SH reagents used and the inhibition of the enzyme activity in the blood serum. With mercurials it was shown that the most reactive -SH groups of the rat blood serum are not related to the X.O. activity, but when sufficient number are reacted the enzyme is structurally altered so that inhibition appears. With oxidants such as iodine the inhibition of the X.O. activity of rat blood serum seems to be not related specifically with the oxidation of -SH groups.
D000818:Animals; D001769:Blood / Q000187:drug effects*; D008297:Male; D051381:Rats; D013439:Sulfhydryl Reagents / Q000494:pharmacology*; D014969:Xanthine Oxidase / Q000037:antagonists & inhibitors* / Q000097:blood
D013439:Sulfhydryl Reagents; D014969:Xanthine Oxidase