Abstract
Modification of the activity of UDP-glucuronyltransferase (UDP-glucuronate glucuronyltransferase (acceptor unspecific), EC 2.4.1.17) by treatment of microsomes with phospholipase A (phosphatide acyl-hydrolase, EC 3.1.1.4) from both Naja naja and Crotalus adamanteus venoms and with p-chloromercuribenzoate has been studied in a variety of species: guinea pig, mouse, rat, beef, rabbit and human. Contrary to reports in the literature that -SH group reagents and phospholipase A inhibit the enzyme, activation of UDP-glucuronyltransferase by these agents was noted in all species examined. Thus, constraint on maximum potential activity is a general property of this enzyme in untreated microsomes from a variety of species. On the other hand, the extent of activation of glucuronyltransferase by treatment of microsomes with phospholipase A or p-chloromercuribenzoate varied with the species studied. In addition to variation in the extent of activation, species differences in the reactivities of the -SH groups associated with UDP-glucuronyltransferase were noted.
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