Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation
Research output: Contribution to journal › Journal article › Research › peer-review
V Niketic, J Thomsen, K Kristiansen
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.
|Journal||European Journal of Biochemistry|
|Number of pages||4|
|Publication status||Published - 1974|
Keywords: Alkanesulfonates; Alkylation; Amino Acids; Autoanalysis; Bromine; Chemical Phenomena; Chemistry; Chromatography, Gas; Chromatography, Ion Exchange; Cysteine; Hydrolysis; Peptides; Proteins; Thiohydantoins