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 chromato...

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Bibliographic Details
Published inPreparative biochemistry Vol. 21; no. 2-3; p. 163
Main Authors Margolin, N, Dee, A, Lai, M, Vlahos, C J
Format Journal Article
LanguageEnglish
Published United States 01.06.1991
Subjects
Chromatography, Agarose
Chromatography, Gel
Chromatography, Ion Exchange
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Escherichia coli - genetics
Gene Products, gag - metabolism
HIV Protease - chemistry
HIV Protease - isolation & purification
Humans
Protein Precursors - metabolism
Recombinant Proteins - chemistry
Recombinant Proteins - isolation & purification
Sepharose - analogs & derivatives
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Summary: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.
ISSN:0032-7484
DOI:10.1080/10826069108018011