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

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.

In: European Journal of Biochemistry, Vol. 46, No. 3, 1974, p. 547-51.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Niketic, V, Thomsen, J & Kristiansen, K 1974, 'Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation', European Journal of Biochemistry, vol. 46, no. 3, pp. 547-51. https://doi.org/10.1111/j.1432-1033.1974.tb03648.x

APA

Niketic, V., Thomsen, J., & Kristiansen, K. (1974). Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation. European Journal of Biochemistry, 46(3), 547-51. https://doi.org/10.1111/j.1432-1033.1974.tb03648.x

Vancouver

Niketic V, Thomsen J, Kristiansen K. Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation. European Journal of Biochemistry. 1974;46(3):547-51. https://doi.org/10.1111/j.1432-1033.1974.tb03648.x

Author

Niketic, V ; Thomsen, J ; Kristiansen, K. / Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation. In: European Journal of Biochemistry. 1974 ; Vol. 46, No. 3. pp. 547-51.

Bibtex

@article{5f4426f013d411de8478000ea68e967b,
title = "Modification of cysteine residues with sodium 2-bromoethanesulfonate. The application of S-sulfoethylated peptides in automatic Edman degradation",
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.",
author = "V Niketic and J Thomsen and K Kristiansen",
note = "Keywords: Alkanesulfonates; Alkylation; Amino Acids; Autoanalysis; Bromine; Chemical Phenomena; Chemistry; Chromatography, Gas; Chromatography, Ion Exchange; Cysteine; Hydrolysis; Peptides; Proteins; Thiohydantoins",
year = "1974",
doi = "10.1111/j.1432-1033.1974.tb03648.x",
language = "English",
volume = "46",
pages = "547--51",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Springer Verlag",
number = "3",

}

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