Sulfenyl Halides as Modifying Reagents for Polypeptides and Proteins. Quantitative Evaluation of Tryptophan and Cysteine Residues in Proteins

作者: Enrico Boccu , Francesco M. Veronese , Angelo Fontana , Carlo A. Benassi

DOI: 10.1111/J.1432-1033.1970.TB00917.X

关键词:

摘要: The determination of tryptophan and cysteine content in proteins by means the selective reaction sulfenyl halides with these amino acids has been carefully investigated. By 2- or 4-nitrophenylsulfenyl chloride aqueous acetic formic acid, nitrophenyl chromophore is covalently bound to residues protein, giving a thioether mixed disulfide respectively. determined spectrophotometrically at 450 nm from 4-nitrothiophenol released disulfides after exposure chloride-labelled protein 0.1 N NaOH (at this wavelength corresponding does not absorb). Tryptophan estimated sulfenylated spectrophotometric determinations 365 328 chromophores (ɛM 4000 11700 respectively), following removal yellow label residues, dissolving modified NaOH. procedure shown be accurate for both wide variety proteins.

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