Abstract
Interactions between purified UDP-glucuronyltransferase from 3-methylcholanthrenetreated rat liver microsomes (named GT-1) and lysophosphatidylcholine, which is essential for expression of GT-1 activity, were examined. Phospholipid-free GT-1, which could not express its full activity [Yokota et al. (1988) J. Biochem. 104, 531-536], was activated fully by addition of lysophosphatidylcholine (0.04mM final concentration) into the assay medium. Lysophosphatidylcholine also protected GT-1 effectively against heat inactivation. Palmitoyllysophosphatidyicholine and stearoyllysophosphatidylcholine were most successful for the activation and stabilization of GT-1.On treatment of GT-1 with earboxypeptidase Y, the transferase was inactivated immediately, but the treatment in the presence of lysophosphatidylcholine affected the activity only a little. Lysophosphatidylcholine was also found to protect GT-1 against cleavage by carboxypeptidase Y. On treatment of GT-1 with trypsin or aminopeptidase T, the activity was lost and GT-1 protein could be digested even when lysophosphatidylcholine was present. It is suggested that UDP-glucuronyltransferase forms an active and stable conformation, in which the carboxyterminal region is protected against protease, with lysophosphatidylcholine.
