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Xenobiotica
the fate of foreign compounds in biological systems
Volume 14, 1984 - Issue 7
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Original Article

Kinetic properties of UDP-glucuronosyltransferase(S) in different membranes of rat liver cells

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Pages 575-579 | Received 28 Nov 1983, Accepted 08 Mar 1984, Published online: 30 Sep 2009
 

Abstract

1. Glucuronidation of 4-nitrophenol, borneol and morphine occurred in rough and smooth endoplasmic reticulum, Golgi apparatus and plasma membranes of rat liver cells.

2. In all fractions, prior fixation of either substrate (UDP-glucuronic acid or the aglycone) enhanced the affinity for the second substrate.

3. Whatever the membrane, glucuronidation of 4-nitrophenol was characterized by high Vmax and high affinity for UDP-glucuronic acid. On the other hand, glucuronidation of borneol exhibited a lower Vmax and a lower affinity for UDP-glucuronic acid.

4. In the endoplasmic reticulum, conjugation of morphine had a low Vmax but the enzyme had high affinities for both UDP-glucuronic acid and the aglycone.

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