Expression in Escherichia coli of the AIDS virus aspartic protease through a protein fusion.
Fusion of the coding sequence for the aspartic protease of HIV-1, the human AIDS virus, to a bacterial beta-lactamase gene, provides an expression system in E. coli which yields high specific activity HIV protease in a soluble form.
Central Research and Development Department DuPont Experimental Station, Wilmington, Delaware 19880-0328.
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Korant
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Rizzo
D016282:Aspartic Acid Endopeptidases; D010450:Endopeptidases / Q000096:biosynthesis / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic; D015967:Gene Expression Regulation, Viral; D006678:HIV / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D010957:Plasmids; D011994:Recombinant Proteins / Q000378:metabolism; D014760:Viral Fusion Proteins / Q000378:metabolism; D001618:beta-Lactamases / Q000096:biosynthesis / Q000235:genetics
D011994:Recombinant Proteins; D014760:Viral Fusion Proteins; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D001618:beta-Lactamases