Kinetic properties of UDP-glucuronosyltransferase(S) in different membranes of rat liver cells.
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.
D000818:Animals; D001892:Camphanes / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D004721:Endoplasmic Reticulum / Q000201:enzymology; D014453:Glucuronosyltransferase / Q000378:metabolism*; D006056:Golgi Apparatus / Q000201:enzymology; D007425:Intracellular Membranes / Q000201:enzymology*; D007700:Kinetics; D008099:Liver / Q000648:ultrastructure*; D008297:Male; D009020:Morphine / Q000378:metabolism; D009596:Nitrophenols / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity; D014535:Uridine Diphosphate Glucuronic Acid / Q000378:metabolism
D001892:Camphanes; D009596:Nitrophenols; D014535:Uridine Diphosphate Glucuronic Acid; D009020:Morphine; D014453:Glucuronosyltransferase; C022871:isoborneol; C024836:4-nitrophenol