期刊论文

Zheng, C.

中文

中华肝脏病杂志

1007-3418

2000

8

6

364-366

10.3760/j.issn:1007-3418.2000.06.015

国家自然科学基金!（39770863） 湖南省自然科学基金!［湘科计字（97）37号-3］

本校为第一机构

目的 进一步了解人醛糖还原酶相似原因（aldose reductase like-1,ARL-1)的功能及其生物学活性，为制备特异性的ARL-1抗体作准备。方法 用基因重组技术构建PQE-ARE-1原核表达载体。在M15大肠杆菌中进行表达，然后利用Ni^+-NTA琼脂柱纯化ARL-1蛋白。结果 经酶切鉴定，PQE-30表达载体上已插入了ARL-1基因，PQE-ARE-1在大肠杆菌中表达产物人重组ARL-1蛋白经纯化后进行SDS-PAGE电泳。成一条蛋白带，分子量为37.7×10^3，表达产物约占全菌蛋白的25%，定量测得ARL-1蛋白的浓度为100mg/L。结论 PQE-ARE-1重组质粒的构建及ARL-1蛋白的制备，为深入研究ARL-1的功能及制备特异性的ARL-1抗体奠定了坚实的基...

OBJECTIVE: To further understand the function and biological activity of aldose reductase like-1 (ARL-1), and to provide the basis for the preparation of the specific antibody against ARL-1. METHODS: The ARL-1 cDNA was cloned into procaryotic expression vector PQE-30 and the recombinant ARL-1 expressed in E.coli M(15); then Ni(+)-NTA agarose columns were used to purify the ARL-1 protein. RESULTS: With the digestion of the enzymes, we identified that the ARL-1 gene was inserted into the procaryotic expression vector PQE-30. The expression products of PQE-ARL-1 (human recombinant ARL-1) showed a...