Kinetic properties of UDP-glucuronosyltransferase(S) in different membranes of rat liver cells
- 1 January 1984
- journal article
- research article
- Published by Taylor & Francis in Xenobiotica
- Vol. 14 (7) , 575-579
- https://doi.org/10.3109/00498258409151451
Abstract
Glucuronidation of 4-nitrophenol, borneol and morphine occurred in rough and smooth endoplasmic reticulum, Golgi apparatus and plasma membranes of rat liver cells. In all fractions, prior fixation of either substrate (UDP-glucuronic acid or the aglycone) enhanced the affinity for the second substrate. 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. 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.Keywords
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