Wooster R, Sutherland L, Ebner T, Clarke D, Da Cruz e Silva O, Burchell B
Biochemical Medicine, University of Dundee, Ninewells Hospital and Medical School, Scotland, U.K.
Biochem J. 1991 Sep 1;278 ( Pt 2)(Pt 2):465-9. doi: 10.1042/bj2780465.
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.
一种新的人肝脏UDP-葡萄糖醛酸基转移酶(HlugP4)已被克隆并在细胞培养中表达。所表达的酶分子量为56 kDa,优先催化卤代和大体积烷基酚的葡萄糖醛酸化反应。该序列的C端一半(246个氨基酸)与HlugP1的相同部分有96%的同一性,而推导的蛋白质序列的N端一半只有38%的同一性。这些结果表明,这两种同工酶可能是由基因产物的差异剪接从同一基因衍生而来。