콘텐츠로 건너뛰기
Merck

Purification of recombinant HIV-1 protease.

Preparative biochemistry (1991-01-01)
N Margolin, A Dee, M Lai, C J Vlahos
초록

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.

MATERIALS
제품 번호
브랜드
제품 설명

Sigma-Aldrich
ω-Aminohexyl–Agarose, saline suspension