Abstract
Recombinant protein expression is of fundamental importance for the production of small or large quantities of biologically active proteins for laboratory and therapeutic uses. The availability of milligram quantities has made elucidation of biological activity and structural characterization possible, even if only small amounts of native protein are available. Commercial insulin, growth hormone, cytokines, and other therapeutic proteins are now produced in large quantities each year using recombinant technologies (1).
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Raftery, M.J. (2000). Characterization of a Mutant Recombinant S100 Protein Using Electrospray Ionization Mass Spectrometry. In: Chapman, J.R. (eds) Mass Spectrometry of Proteins and Peptides. Methods in Molecular Biology™, vol 146. Humana Press, Totowa, NJ. https://doi.org/10.1385/1-59259-045-4:27
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DOI: https://doi.org/10.1385/1-59259-045-4:27
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