cDNA cloning and expression analysis of the human UDPglucose dehydrogenase.

H L Peng, M D Lou, M L Chang, H Y Chang
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Abstract

A cDNA clone encoding the human UDPglucose dehydrogenase was isolated from a liver cDNA library. The cDNA is 2,355 bp in length with an open reading frame which is capable of encoding a protein of 494 residues. The predicted primary sequence of the gene product is in good agreement with that of the bovine enzyme determined previously found by means of protein sequencing. Two major transcripts of the UDPglucose dehydrogenase gene with sizes of 2.8 and 2.35 kb, respectively, were observed by Northern analysis. The gene was found to be expressed in a variety of tissues with the highest level in liver, consistent with the physiological function of the enzyme in excretion of endo- and xenobiotics compounds.

人类 UDP 葡萄糖脱氢酶的 cDNA 克隆和表达分析。
从肝脏 cDNA 文库中分离出了编码人类 UDP 葡萄糖脱氢酶的 cDNA 克隆。cDNA 长度为 2,355 bp,具有开放阅读框,能编码 494 个残基的蛋白质。预测的基因产物主序列与之前通过蛋白质测序发现的牛酶的主序列十分吻合。通过 Northern 分析,观察到 UDP 葡萄糖脱氢酶基因的两个主要转录本,大小分别为 2.8 kb 和 2.35 kb。该基因在多种组织中都有表达,肝脏中的表达量最高,这与该酶排泄内源性和外源性化合物的生理功能相一致。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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