Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation

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A procedure for alkylation of cysteine residues with sodium 2-bromoethanesulfonate is described. The reaction is performed under mild conditions and complete modification is obtained without side reactions.

S-Sulfoethylated proteins are comparable to performic acid oxidized or S-sulfonated proteins with respect to solubility properties and behaviour in ion exchange chromatography. S-Sulfoethylcysteine was found to be stable during acid hydrolysis. S-Sulfoethylated peptides were suitable for automatic Edman degradation due to their polarity, since losses during extraction are reduced, especially after the coupling stage, as shown by degradation of modified peptides.

Original languageEnglish
JournalEuropean Journal of Biochemistry
Issue number3
Pages (from-to)547-51
Number of pages4
Publication statusPublished - 1974
Externally publishedYes

Bibliographical note

Keywords: Alkanesulfonates; Alkylation; Amino Acids; Autoanalysis; Bromine; Chemical Phenomena; Chemistry; Chromatography, Gas; Chromatography, Ion Exchange; Cysteine; Hydrolysis; Peptides; Proteins; Thiohydantoins

ID: 11368686