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.