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• W2079749468 abstract "Various constructs of the human immunodeficiency virus, type 1 (HIV-1) protease containing flanking Pol region sequences were expressed as fusion proteins with the maltose-binding protein of the malE gene of Escherichia coli. The full-length fusion proteins did not exhibit self-processing in E. coli, thereby allowing rapid purification by affinity chromatography on cross-linked amylose columns. Denaturation of the fusion protein in 5 M urea, followed by renaturation, resulted in efficient site-specific autoprocessing to release the 11-kDa protease. Rapid purification involving two column steps gave an HIV-1 protease preparation of > 95% purity (specific activity ∼ 8500 pmol · min−1·μg protease−1) with an overall yield of about 1 mg/l culture. Incubation of an inactive mutant protease fusion protein with the purified wild-type protease resulted in specific trans cleavage and release of the mutant protease. Analysis of products of the HIV-1 fusion proteins containing mutations at either the N-or the C-terminal protease cleavage sites indicated that blocking one of the cleavage sites influences the cleavage at the non-mutated site. Such mutated full-length and truncated protease fusion proteins possess very low levels of proteolytic activity (∼ 5 pmol · min−1·μg protein−1)." @default.
• W2079749468 created "2016-06-24" @default.
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• W2079749468 date "1991-07-01" @default.
• W2079749468 modified "2023-09-26" @default.
• W2079749468 title "Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli" @default.
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• W2079749468 doi "https://doi.org/10.1111/j.1432-1033.1991.tb16132.x" @default.
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