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• W2419235280 abstract "Several protease IV enzymes are widely used in proteomic research. Specifically, protease IV from Pseudomonas aeruginosa has lysyl endopeptidase activity. Here, we report the recombinant expression, refolding, activation, and purification of this protease in Escherichia coli. Proteolytic instability of the activated intermediate, a major obstacle for efficient production, is controlled through ammonium sulfate precipitation. The purified protease IV exhibits superior lysyl endopeptidase activity compared to a commercial product." @default.
• W2419235280 created "2016-06-24" @default.
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• W2419235280 date "2016-10-01" @default.
• W2419235280 modified "2023-10-17" @default.
• W2419235280 title "Recombinant expression, refolding, purification and characterization of Pseudomonas aeruginosa protease IV in Escherichia coli" @default.
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• W2419235280 doi "https://doi.org/10.1016/j.pep.2016.05.019" @default.
• W2419235280 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27260967" @default.
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