scholarly journals An improved assay technique for uridine diphosphate glucuronosyltransferase activity towards 5-hydroxytryptamine and some properties of the enzyme

1978 ◽  
Vol 175 (3) ◽  
pp. 1119-1124 ◽  
Author(s):  
J E A Leakey
Keyword(s):  
Rat Liver ◽  
Mouse Liver ◽  
Wistar Rat ◽  
Uridine Diphosphate ◽  
Gunn Rat ◽  
Uridine Diphosphate Glucuronosyltransferase ◽  
Membrane Perturbation ◽  
Udp Glucuronosyltransferase ◽  
Routine Assay ◽  
Assay Technique

A simplified and sensitive procedure for the routine assay of UDP-glucuronosyltransferase activity towards 5-hydroxytryptamine (serotonin) was developed and the reaction product confirmed as the O-glucuronide of this substrate. The assay was used to study some properties of this UDP-glucuronosyltransferase activity. In mouse liver activity was stimulated by membrane-perturbation procedures and by UDP-N-acetylglucosamine. In rat liver it was stimulated by digitonin, but not by diethylnitrosamine. Mouse duodenum, kidney, and lung possessed activity that was less latent than in liver. No activity was found in homogenates of brain. The activity was present in Gunn rat liver, though only one-third of that in Wistar rat liver. Cat liver contained no UDP-glucuronosyltransferase activity towards 5-hydroxytryptamine.

scholarly journals Stimulation of defective Gunn-rat liver uridine diphosphate glucuronyltransferase activity in vitro by alkyl ketones

1979 ◽  
Vol 177 (3) ◽  
pp. 993-995 ◽  
Author(s):  
E N Lalani ◽  
B Burchell
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Wistar Rat ◽  
Uridine Diphosphate ◽  
Gunn Rat ◽  
Alkyl Ketone ◽  
Genetic Deficiency ◽  
Liver Homogenates ◽  
Stimulation Of

Addition of alkyl ketone (10mM) to Gunn-rat liver homogenates increased UDP-glucuronyltransferase activity towards 2-aminophenol by 10–20 fold, up to enhanced values of enzyme activity observed with similarly treated Wistar-rat liver homogenates. Alkyl ketones also activate the defective enzyme purified from Gunn-rat liver. This genetic deficiency of UDP-glucuronyltransferase activity is no longer apparent when assayed in the presence of alkyl ketones.

scholarly journals Reconstitution of purified Wistar rat liver bilirubin UDP-glucuronyltransferase into Gunn-rat liver microsomes

1982 ◽  
Vol 201 (3) ◽  
pp. 653-656 ◽  
Author(s):  
B Burchell
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Specific Activity ◽  
Liver Microsomes ◽  
Wistar Rat ◽  
Transferase Activity ◽  
Rat Liver Microsomes ◽  
Phosphatidylcholine Liposomes ◽  
Gunn Rat ◽  
Rigid Environment

1. Reconstitution of purified bilirubin UDP-glucuronyltransferase from Wistar-rat liver into Gunn-rat liver microsomes provides a better environment than phosphatidylcholine liposomes, such that the final specific activity of the Wistar-rat liver enzyme was increased up to 85 units/mg of protein. 2. Gunn- and Wistar-rat liver microsomes were equally effective for reconstitution of the purified enzyme. 3. The transferase activity does not appear to be fully expressed in the more rigid environment of foetal Wistar-rat liver microsomes. 4. These reconstitution experiments reveal a final specific activity for the purified bilirubin UDP-glucuronyltransferase consistent with the capacity of the whole rat liver to glucuronidate bilirubin and indicate that the absence of this enzyme activity in Gunn-rat liver microsomes is not due to an abnormal microenvironment.

Adenovirus-Mediated Gene Therapy to Restore Expression and Functionality of Multiple UDP-Glucuronosyltransferase 1A Enzymes in Gunn Rat Liver

2006 ◽  
Vol 318 (3) ◽  
pp. 1240-1247 ◽  
Author(s):  
Kristini K. Miles ◽  
Fay K. Kessler ◽  
Laura J. Webb ◽  
Philip C. Smith ◽  
Joseph K. Ritter
Keyword(s):  
Gene Therapy ◽  
Rat Liver ◽  
Gunn Rat ◽  
Udp Glucuronosyltransferase

scholarly journals Demonstration of functional heterogeneity of hepatic uridine diphosphate glucuronosyltransferase activities after administration of 3-methylcholanthrene and phenobarbital to rats

1978 ◽  
Vol 174 (2) ◽  
pp. 671-672 ◽  
Author(s):  
G J Wishart
Keyword(s):  
Adult Male ◽  
The Other ◽  
Male Rats ◽  
Uridine Diphosphate ◽  
Functional Heterogeneity ◽  
Uridine Diphosphate Glucuronosyltransferase ◽  
Udp Glucuronosyltransferase ◽  
Phenobarbital Administration ◽  
Relationship Of ◽  
The Relationship

After the administration of 3-methylcholanthrene to adult male rats, activities of hepatic UDP-glucuronosyltransferase towards six from a group of 12 substrates were stimulated by 250-350%. Activities towards the remaining six substrates were unaffected. Conversely, after phenobarbital administration, activities formerly stimulated by 3-methylcholanthrene remained unchanged, and the other six activities were stimulated by 160-280%. The relationship of these two groups of transferase activities to other evidence suggesting the same heterogeneity of the enzyme is discussed.

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

1980 ◽  
Vol 191 (1) ◽  
pp. 155-163 ◽  
Author(s):  
P J Weatherill ◽  
S M Kennedy ◽  
B Burchell
Keyword(s):  
Rat Liver ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Wistar Rat ◽  
Rat Strains ◽  
Gunn Rat ◽  
Genetic Deficiency ◽  
Rat Livers

1. Antiserum was raised against purified Wistar-rat liver UDP-glucuronyltransferase. 2. UDP-glucuronyltransferase activities towards 4-nitrophenol, bilirubin, 1-naphthol and morphine were co-immunoprecipitated from solubilized Wistar-rat liver preparations. 3. UDP-glucuronyltransferase activities towards 1-naphthol, 2-aminophenol and 4-nitrophenol were precipitated from solubilized Gunn-rat liver preparations by this antiserum. 4. UDP-glucuronyltransferase activities towards 1-naphthol, 4-nitrophenol and bilirubin, from Wistar-rat liver, were slightly inhibited by antiserum, whereas 1-naphthol UDP-glucuronyltransferase activity from Gunn-rat livers was greatly inhibited. 5. Measurable Wistar-rat liver glucuronyltransferase activities in washed immunoprecipitates indicate that the enzyme(s) were not merely inhibited by antiserum. 6. Immunoglobulin G purified from this antiserum immunoprecipitated transferase activities towards 4-nitrophenol, bilirubin and 1-naphthol. 7. The washed immunoprecipitates from both rat strains, containing UDP-glucuronyltransferase activity, appear to be similar when analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 8. Radial-immunodiffusion studies suggest that a smaller amount of UDP-glucuronyltransferase protein is present in Gunn-rat liver than in Wistar-rat liver. 9. The significance of these results in relation to the genetic deficiency in the Gunn rat is discussed.

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