Purification of Recombinant HIV-1 Protease |
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| Authors: | Nara Margolin Albert Dee Mei Lai Chris J Vlahos |
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| Institution: | Lilly Research Laboratories , Indianapolis, IN, 46285 |
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| Abstract: | 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 μg 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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