Nuclear membrane-bound UDPglucuronosyltransferase of rat liver

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Abstract
Some properties of rat liver nuclear membrane-bound UDP-glucuronosyltransferase were compared with those of the endoplasmic reticulum bound enzyme. The activity of nuclear membrane-bound UDP-glucuronosyltransferase was stimulated only about 1.5-fold by Lubrol WX. Under the same conditions microsomal UDP-glucuronosyltransferase was, as usual, highly activated (up to 10-fold), when 4-nitrophenol was the acceptor of glucuronic acid. Specific activities of the detergent-activated enzyme were similar in microsomal and nuclear membrane preparations, when the following aglycone substrates were used 4-methylumbelliferone, 4-nitrophenol, 1-naphthol, phenolphthalein, and testosterone. Apparent Km values for UDP-glucuronic acid ranged between 0.15-0.25 mM for glucuronidation of 4-nitrophenol and 1-naphthol, by either Lubrol WX activated or non-activated, nuclear membrane-bound UDP-glucuronosyltransferase. These values were comparable to those found for detergent-activated microsomal enzyme. The results show a similarity in behavior of detergent-activated UDP-glucuronosyltransferase regardless of subcellular membrane source and, therefore, suggest the association of the same glucuronyltransferase with nuclear membrane and endoplasmic reticulum. A possible significance of the presence of high activity of this enzyme in nuclear membrane is discussed.