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• W2037576809 abstract "A secreted, soluble variant of the Kex-1 endopeptidase from Kluyveromyces lactis has been produced and studied as a novel cleavage enzyme exhibiting high specificity for the Lys-Arg peptide. This highly selective, efficient enzyme is particularly adapted for use in manufacturing when a recombinant therapeutic protein, possessing its native N-terminus, has to be released in vitro from a bacterially-expressed fusion protein. In this paper, we describe the preparation of a Kex-1 variant using Saccharomyces cerevisiae and its application in the production of important therapeutic recombinant proteins such as human growth hormone, granulocyte colony-stimulating factor and interferon-alpha-2b." @default.
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• W2037576809 date "2008-06-01" @default.
• W2037576809 modified "2023-10-17" @default.
• W2037576809 title "Efficient bacterial expression of fusion proteins and their selective processing by a recombinant Kex-1 protease" @default.
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• W2037576809 doi "https://doi.org/10.1016/j.pep.2008.02.018" @default.
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