Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family

R. Wooster; L. Sutherland; T. Ebner; D. Clarke; E. O. Da Cruz Silva; B. Burchell

doi:10.1042/bj2780465

Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family

R. Wooster, L. Sutherland, T. Ebner, D. Clarke, E. O. Da Cruz Silva, B. Burchell

Research output: Contribution to journal › Article › peer-review

137 Citations (Scopus)

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.

Original language	English
Pages (from-to)	465-469
Number of pages	5
Journal	Biochemical Journal
Volume	278
Issue number	2
DOIs	https://doi.org/10.1042/bj2780465
Publication status	Published - 1 Sep 1991
Externally published	Yes

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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.",

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AU - Sutherland, L.

AU - Ebner, T.

AU - Clarke, D.

AU - Da Cruz Silva, E. O.

AU - Burchell, B.

PY - 1991/9/1

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AB - 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.

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Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family

Abstract

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