Abstract
Low concentrations of the detergents Triton X-100 and deoxycholate enhanced the activity of rat liver microsomal p-nitrophenol glucuronyltransferase 3-fold without radically altering the activities of pyrophosphatase or β-glucuronidase. Similar concentrations of the detergents, however, had no significant activating effect on the glucuronyltransferase activity of guinea pig liver microsomal fractions prepared in identical manner. Triton X-100 still activated the rat liver enzyme when competition between glucuronyltransferase and pyrophosphatase for UDP-glucuronate was reduced at a higher concentration of the sugar nucleotide and when β-glucuronidase had been substantially inhibited with saccharo-1,4-lactone. It is concluded that the closely associated pyrophosphatase and β-glucuronidase activities are not involved in the activation of the rat liver enzyme by detergents. The activation of rat liver glucuronyltransferase and the differences between that enzyme and guinea pig liver glucuronyltransferase are discussed.
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