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  • Title: Large-scale production of HIV-1 protease from Escherichia coli using selective extraction and membrane fractionation.
    Author: Gustafson ME, Junger KD, Foy BA, Baez JA, Bishop BF, Rangwala SH, Michener ML, Leimgruber RM, Houseman KA, Mueller RA.
    Journal: Protein Expr Purif; 1995 Aug; 6(4):512-8. PubMed ID: 8527938.
    Abstract:
    Human immunodeficiency virus type 1 (HIV-1) protease was expressed in Escherichia coli as a fusion protein with the N-terminal sequence of IGF-2. The protein accumulated in inclusion bodies as a 40:60 mixture of unprocessed fusion protein and processed protein. A simple purification procedure was developed that yielded 30-40 mg of active protease per liter of fermentation broth with a recovery of 30-40%. The purification process involved the selective extraction of HIV-1 protease from E. coli inclusion bodies with 50% acetic acid and fractional diafiltration to remove impurities and low-molecular-weight protease-related fragments. No chromatographic steps were employed, yet the HIV-1 protease produced by this procedure was greater than 95% pure by SDS-PAGE, reverse-phase HPLC, and N-terminal sequence analysis.
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