Separation of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase activities

Abstract

Rabbit liver UDP-glucuronyltransferase activity was resolved into two separate fractions on DEAE-cellulose, one containing most of the transferase activity toward oestrone and the other most of the activity toward p-nitrophenol. These two activities were completely separated by rechromatography of each fraction on a second DEAE-cellulose column.

Strain differences in rat liver (UDP-glucuronyltransferase activity towards androsterone

“…Recently evidence for the heterogeneity of UDPglucuronyltransferase has accumulated on the basis of inducibility (Dutton & Burchell, 1977), agedependent development (Fuchs et al, 1977;Lucier & McDaniel, 1977;Wishart, 1978), chromatographic separation (Bock et al, 1977;Tukey et al, 1978) and substrate specificity of the purified transferase (Burchell, 1978), though androsterone was not among the substrates examined. The purified transferase was phospholipidor detergent-dependent (Burchell & Hallinan, 1978) and its deficiency towards 2-aminophenol in the Gunn strain of rat could be repaired by addition of diethylnitrosaniine (Weatherill & Burchell, 1978), suggesting an interaction with the enzyme protein itself or with its linkage to detergent or phospholipid (Weatherill & Burchell, 1978).…”

Induction and Inhibition of Cytochrome P450 and Drug-Metabolizing Enzymes by Climbazole.

“…23) Glutathione S-transferase activity against 1-chloro-2,4-dinitrobenzene was assayed spectrophotometrically according to the method of Habig and Jakoby. 24) Microsomal UDP-glucuronosyl transferase activity against pnitrophenol was determined spectrophotometrically from the disappearance of 4-nitrophenol according to the method of Tukey et al 25) Protein concentration was estimated by the method of Lowry et al 26) using bovine serum albumin as the standard.…”

Immunochemical comparison of UDP-glucuronyltransferase from Gunn- and Wistar-rat livers

“…However, different forms of UDPglucuronyltransferase that have very similar molecular weights would not be detected by these immunochemical experiments. Multiple forms of UDP-glucuronyltransferase may exist, but may only be separable on a charge basis such as DEAEcellulose chromatography (Del Villar et al, 1977;Tukey et al, 1978). More recently, Bock et al (1979) have reported that morphine UDP-glucuronyltransferase may have a slightly higher mol.wt.…”