Abstract
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.
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Dates
Type | When |
---|---|
Created | 20 years, 6 months ago (March 4, 2005, 8:40 a.m.) |
Deposited | 1 year, 9 months ago (Nov. 22, 2023, 4:41 p.m.) |
Indexed | 2 days, 1 hour ago (Sept. 4, 2025, 9:48 a.m.) |
Issued | 51 years, 1 month ago (Aug. 1, 1974) |
Published | 51 years, 1 month ago (Aug. 1, 1974) |
Published Online | 20 years, 6 months ago (March 3, 2005) |
Published Print | 51 years, 1 month ago (Aug. 1, 1974) |
@article{NIKETIC_1974, title={Modification of Cysteine Residues with Sodium 2‐Bromoethanesulfonate: The Application of S‐Sulfoethylated Peptides in Automatic Edman Degradation}, volume={46}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1974.tb03648.x}, DOI={10.1111/j.1432-1033.1974.tb03648.x}, number={3}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={NIKETIC, Vesna and THOMSEN, Johannes and KRISTIANSEN, Karsten}, year={1974}, month=aug, pages={547–551} }