Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2021637 | Protein Expression and Purification | 2008 | 8 Pages |
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-α-2b.
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Authors
Sabrina Pozzuolo, Umberto Breme, Barbara Salis, Geoffrey Taylor, Giancarlo Tonon, Gaetano Orsini,