title: Properties of lubrol-extracted uridine diphosphate glucuronyltransferase.
abstract: 1. A partially purified UDP-glucuronyltransferase was obtained by extracting rat liver microsomal preparations with Lubrol, a non-ionic detergent. 2. The soluble enzyme catalysed conjugation of both o-aminophenol and p-nitrophenol and was extremely stable when compared with untreated microsomal preparations. 3. The characteristics of the conjugation of the two phenols were found to differ with respect to pH optimum, bivalent cation requirement and Michaelis constants, suggesting that more than one enzyme is involved in the conjugation reaction.
mesh_terms: D000818:Animals; D002118:Calcium; D002501:Centrifugation, Zonal; D003902:Detergents; D005027:Ethylene Oxide; D005965:Glucuronates; D006602:Hexosyltransferases / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008274:Magnesium; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D009596:Nitrophenols; D010636:Phenols; D051381:Rats; D012995:Solubility; D013997:Time Factors; D014461:Ultracentrifugation
chemical_list: D003902:Detergents; D005965:Glucuronates; D009596:Nitrophenols; D010636:Phenols; D006602:Hexosyltransferases; D008274:Magnesium; D005027:Ethylene Oxide; D002118:Calcium