Purification of recombinant HIV-1 protease. |
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Authors: | N Margolin A Dee M Lai C J Vlahos |
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Affiliation: | Lilly Research Laboratories, Indianapolis, IN 46285. |
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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. |
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