Purification of recombinant HIV-1 protease.
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.
Margolin
N
N
Lilly Research Laboratories, Indianapolis, IN 46285.
Dee
A
A
Lai
M
M
Vlahos
C J
CJ
D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D015683:Gene Products, gag / Q000378:metabolism; D016333:HIV Protease / Q000737:chemistry / Q000302:isolation & purification*; D006801:Humans; D011498:Protein Precursors / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012685:Sepharose / Q000031:analogs & derivatives
D015683:Gene Products, gag; D011498:Protein Precursors; D011994:Recombinant Proteins; C059767:p55 gag precursor protein, Human immunodeficiency virus 1; C024903:aminohexyl-sepharose; D012685:Sepharose; D016333:HIV Protease