Peng H L, Lou M D, Chang M L, Chang H Y
Institute of Biological Science and Technology, National Chiao-Tung University, Hsin Chu, Taiwan, R.O.C.
Proc Natl Sci Counc Repub China B. 1998 Oct;22(4):166-72.
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.
从人肝脏cDNA文库中分离出一个编码人尿苷二磷酸葡萄糖脱氢酶的cDNA克隆。该cDNA长度为2355bp,具有一个开放阅读框,能够编码一个由494个氨基酸残基组成的蛋白质。通过蛋白质测序先前确定的该基因产物的预测一级序列与牛酶的序列高度一致。通过Northern分析观察到尿苷二磷酸葡萄糖脱氢酶基因有两种主要转录本,大小分别为2.8kb和2.35kb。发现该基因在多种组织中表达,在肝脏中表达水平最高,这与该酶在排泄内源性和外源性化合物中的生理功能一致。