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Royal Society of Chemistry, Organic and Biomolecular Chemistry, 21(6), p. 3977, 2008

DOI: 10.1039/b811501j

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Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation

Journal article published in 2008 by Jonathan P. Richardson ORCID, Derek Macmillan
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

Selective protein cleavage at methionine residues is a useful method for the production of bacterially derived protein fragments containing an N-terminal cysteine residue required for native chemical ligation. Here we describe an optimised procedure for cyanogen bromide-mediated protein cleavage, and ligation of the resulting fragments to afford biologically active proteins.