Isolation of an activator of bilirubin glucuronyltransferase from normal and jaundiced Gunn rats.
A microsomal activator of the UDP-glucuronyltransferase for bilirubin has been isolated from lubrol solubilized and salt fractionated liver microsomes. The activator has been partially purified by anion exchange and molecular sieving chromatography and found to have a molecular weight of about 60 kDa. The activator is present in liver from normal and bilirubin UDP-glucuronyltransferase deficient Gunn rats. When tested with purified UDP-glucuronyltransferase for bilirubin it accelerated the conjugation rate 10 fold but with the purified UDP-paranitrophenol transferase the rate of conjugation was increased only 1.5 times.
Odell
G B
GB
Department of Pediatrics, University of Wisconsin School of Medicine, Madison 53792.
Mogilevsky
W S
WS
Siegel
F L
FL
D000818:Animals; D004789:Enzyme Activation; D014453:Glucuronosyltransferase; D006602:Hexosyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D007565:Jaundice / Q000201:enzymology*; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology*; D011506:Proteins / Q000302:isolation & purification / Q000502:physiology*; D051381:Rats; D011911:Rats, Gunn; D012016:Reference Values
D011506:Proteins; C019787:bilirubin glucuronoside glucuronosyltransferase; D006602:Hexosyltransferases; D014453:Glucuronosyltransferase