Characterisation of a human bilirubin UDP-glucuronosyltransferase stably expressed in hamster lung fibroblast cell cultures

A cDNA encoding a human bilirubin UDP-glucuronosyltransferase has been isolated and stably expressed in Chinese hamster V79 lung fibroblast cell line. Western blotting of cell homogenates with anti-UGT antibody revealed a highly expressed protein of approx. 55.5 kDa in size. The expressed enzyme spe...

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Bibliographic Details
Published in:FEBS letters 1992-08, Vol.308 (2), p.161-164
Main Authors: Sutherland, Lesley, Senafi, Sahidan bin, Ebner, Thomas, Clarke, Douglas J., Burchell, Brian
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
bilirubin UDP-glucuronosyltransferase
Biological and medical sciences
Blotting, Western
cDNA
Cells, Cultured
Chromatography, High Pressure Liquid
Complementary DNA
Cricetinae
Cricetulus
DNA
enzymatic activity
Enzyme activity
Enzymes and enzyme inhibitors
Eukaryotic expression vector
expression
Fundamental and applied biological sciences. Psychology
Gene Expression
Glucuronosyltransferase
Hexosyltransferases - genetics
Hexosyltransferases - metabolism
Humans
Isoenzymes - genetics
Isoenzymes - metabolism
Lung - cytology
Lung - metabolism
man
Microsomes, Liver - enzymology
Plasmids
Substrate Specificity
Transferases
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Summary:A cDNA encoding a human bilirubin UDP-glucuronosyltransferase has been isolated and stably expressed in Chinese hamster V79 lung fibroblast cell line. Western blotting of cell homogenates with anti-UGT antibody revealed a highly expressed protein of approx. 55.5 kDa in size. The expressed enzyme specifically catalysed the formation of bilirubin mono- and diglucuronides, and also catalysed the glucuronidation of two phenolic compounds, which are good substrates for other human UGT isoenzymes, at low rates.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)81266-O