Preparative biochemistry 1991-01-01

Purification of recombinant HIV-1 protease.

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

Index: Prep. Biochem. 21(2-3) , 163-73, (1991)

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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.