Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Standard
Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation. / Niketic, V; Thomsen, J; Kristiansen, K.
I: European Journal of Biochemistry, Bind 46, Nr. 3, 1974, s. 547-51.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation
AU - Niketic, V
AU - Thomsen, J
AU - Kristiansen, K
N1 - Keywords: Alkanesulfonates; Alkylation; Amino Acids; Autoanalysis; Bromine; Chemical Phenomena; Chemistry; Chromatography, Gas; Chromatography, Ion Exchange; Cysteine; Hydrolysis; Peptides; Proteins; Thiohydantoins
PY - 1974
Y1 - 1974
N2 - 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.
AB - 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.
U2 - 10.1111/j.1432-1033.1974.tb03648.x
DO - 10.1111/j.1432-1033.1974.tb03648.x
M3 - Journal article
C2 - 4368921
VL - 46
SP - 547
EP - 551
JO - FEBS Journal
JF - FEBS Journal
SN - 1742-464X
IS - 3
ER -
ID: 11368686