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.
| Original language | English |
|---|---|
| Journal | European Journal of Biochemistry |
| Volume | 46 |
| Issue number | 3 |
| Pages (from-to) | 547-51 |
| Number of pages | 4 |
| ISSN | 0014-2956 |
| DOIs | |
| Publication status | Published - 1974 |
| Externally published | Yes |