Demonstration of functional heterogeneity of hepatic uridine diphosphate glucuronosyltransferase activities after administration of 3-methylcholanthrene and phenobarbital to rats
- 15 August 1978
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 174 (2), 671-672
- https://doi.org/10.1042/bj1740671
Abstract
After the administration of 3-methylcholanthrene to adult male rats, activities of hepatic UDP-glucuronosyltransferase (EC 2.4.1.17) towards 6 from a group of 12 substrates were stimulated by 250-350%. Activities towards the remaining 6 substrates were unaffected. Conversely, after phenobarbital administration, activities formerly stimulated by 3-methylcholanthrene remained unchanged, and the other 6 activities were stimulated by 160-280%. The relationship of these 2 groups of transferase activities to other evidence suggesting the same heterogeneity of the enzyme is discussed.This publication has 4 references indexed in Scilit:
- Functional heterogeneity of UDP-glucuronosyltransferase as indicated by its differential development and inducibility by glucocorticoids. Demonstration of two groups within the enzyme's activity towards twelve substratesBiochemical Journal, 1978
- Steroid and non-steroid UDP glucuronyltransferase: Glucuronidation of synthetic estrogens as steroidsThe Journal of Steroid Biochemistry and Molecular Biology, 1977
- Differential stimulation of foetal rat liver uridine diphosphate glucuronyltransferase activity towards certain substrates after glucocorticoid treatment in culture and in utero, and during natural development [proceedings].1977
- Effects of phenobarbital and 3-methylcholanthrene on substrate specificity of rat liver microsomal UDP-glucuronyltransferaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1973