重组HIV-1蛋白酶的纯化

Purification of recombinant HIV-1 protease.

作者信息

Margolin N, Dee A, Lai M, Vlahos C J

机构信息

Lilly Research Laboratories, Indianapolis, IN 46285.

出版信息

Prep Biochem. 1991;21(2-3):163-73. doi: 10.1080/10826069108018011.

DOI:10.1080/10826069108018011

PMID:1798693

Abstract

A method is described to purify recombinant HIV-1 protease from soluble extracts of Escherichia coli. The isolation involves QAE-Sepharose anion exchange chromatography, hexyl agarose hydrophobic interaction chromatography, MonoS cation exchange chromatography, and Superose 6 size exclusion chromatography. Approximately 100 micrograms of protease was obtained from 18 g E. coli paste. The protein was judged to be homogeneous due to the presence of a single band on a silver-stained SDS polyacrylamide gel.

摘要

描述了一种从大肠杆菌可溶性提取物中纯化重组HIV-1蛋白酶的方法。该分离过程包括QAE-琼脂糖阴离子交换色谱、己基琼脂糖疏水相互作用色谱、MonoS阳离子交换色谱和Superose 6尺寸排阻色谱。从18克大肠杆菌菌泥中获得了约100微克蛋白酶。由于在银染的SDS聚丙烯酰胺凝胶上出现单一条带，判断该蛋白质是纯的。