Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family
- 1 September 1991
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 278 (2), 465-469
- https://doi.org/10.1042/bj2780465
Abstract
A new human liver UDP-glucuronosyltransferase (HlugP4) has been cloned and expressed in cell culture. The expressed enzyme has a molecular mass of 56 kDa and preferentially catalysed the glucuronidation of halogenated and bulky alkyl phenols. The C-terminal half of the sequence (246 amino acids) is 96% identical with the same portion of HlugP1, whereas the N-terminal half of the deduced protein sequences are only 38% identical. These results suggest that the two isoenzymes may be derived from the same gene by differential splicing of the gene product.Keywords
This publication has 28 references indexed in Scilit:
- Assessment of the drug inhibitor specificity of the human liver 4-methylumbelliferone UDP-glucuronosyltransferase activityBiochemical Pharmacology, 1991
- NADPH-cytochrome P-450 oxidoreductase gene organization correlates with structural domains of the proteinBiochemistry, 1990
- UDP-glucuronosyltransferases: a family of detoxifying enzymesTrends in Pharmacological Sciences, 1990
- Isolation and sequencing of rat liver bilirubin UDP-glucuronosyltransferase cDNA: Possible alternate splicing of a common primary transcriptBiochemical and Biophysical Research Communications, 1990
- Chromosomal mapping of a human phenol UDP-glucuronosyltransferase, GNT1Annals of Human Genetics, 1990
- UDP-glucuronosyltransferasesPharmacology & Therapeutics, 1989
- Expression of a human liver cDNA encoding a UDP‐glucuronosyltransferase catalysing the glucuronidation of hyodeoxycholic acid in cell cultureFEBS Letters, 1989
- Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA PolymeraseScience, 1988
- Expression of functional acetylcholine receptor from cloned cDNAsNature, 1984
- Detection of specific sequences among DNA fragments separated by gel electrophoresisJournal of Molecular Biology, 1975