The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Activation and Stabilization of UDP-Glucuronyltransferase by Lysophosphatidylcholine
Hiroshi YokotaAkira Yuasa
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1992 Volume 112 Issue 3 Pages 309-313

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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.

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