Abstract
If cysteine and cystine are identified in proteins, they will require modification before they can be quantified. Oxidation to cysteic acid is still commonly used with postcolumn amino acid analyzers employing ion-exchange resins and ninhydrin detection. Oxidation with performic acid converts cysteine and cystine to cysteic acid and methionine to methionine sulfone. Tryptophan is also modified during the oxidation procedure by indole ring opening to form N-formylkynurenine and other products. Tyrosine may become halogenated if, for example, traces of bromide or chloride ions are present. The yield of cysteic acid is 90%, whereas 100% oxidation of Met to the sulfone is achieved.
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© 1994 Humana Press Inc., Totowa, NJ
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Aitken, A. (1994). Analysis of Cysteine Residues and Disulfide Bonds. In: Walker, J.M. (eds) Basic Protein and Peptide Protocols. Methods in Molecular Biology™, vol 32. Humana Press. https://doi.org/10.1385/0-89603-268-X:351
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DOI: https://doi.org/10.1385/0-89603-268-X:351
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