Identification of thioredoxin target disulfides using isotope-coded affinity tags

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Standard

Identification of thioredoxin target disulfides using isotope-coded affinity tags. / Hägglund, Per; Bunkenborg, Jakob; Maeda, Kenji; Finnie, Christine; Svensson, Birte.

Plant Proteomics. ed. / Jesus V. Jorrin-Novo. Humana Press, 2014. p. 677-685 (Methods in Molecular Biology, Vol. 1072).

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Harvard

Hägglund, P, Bunkenborg, J, Maeda, K, Finnie, C & Svensson, B 2014, Identification of thioredoxin target disulfides using isotope-coded affinity tags. in JV Jorrin-Novo (ed.), Plant Proteomics. Humana Press, Methods in Molecular Biology, vol. 1072, pp. 677-685. https://doi.org/10.1007/978-1-62703-631-3_47

APA

Hägglund, P., Bunkenborg, J., Maeda, K., Finnie, C., & Svensson, B. (2014). Identification of thioredoxin target disulfides using isotope-coded affinity tags. In J. V. Jorrin-Novo (Ed.), Plant Proteomics (pp. 677-685). Humana Press. Methods in Molecular Biology Vol. 1072 https://doi.org/10.1007/978-1-62703-631-3_47

Vancouver

Hägglund P, Bunkenborg J, Maeda K, Finnie C, Svensson B. Identification of thioredoxin target disulfides using isotope-coded affinity tags. In Jorrin-Novo JV, editor, Plant Proteomics. Humana Press. 2014. p. 677-685. (Methods in Molecular Biology, Vol. 1072). https://doi.org/10.1007/978-1-62703-631-3_47

Author

Hägglund, Per ; Bunkenborg, Jakob ; Maeda, Kenji ; Finnie, Christine ; Svensson, Birte. / Identification of thioredoxin target disulfides using isotope-coded affinity tags. Plant Proteomics. editor / Jesus V. Jorrin-Novo. Humana Press, 2014. pp. 677-685 (Methods in Molecular Biology, Vol. 1072).

Bibtex

@inbook{71809ce650d34ed79806e4952e960ab7,
title = "Identification of thioredoxin target disulfides using isotope-coded affinity tags",
abstract = "Thioredoxins (Trx) are small redox proteins that reduce disulfide bonds in various target proteins and maintain cellular thiol redox control. Here, a thiol-specific labeling and affinity enrichment approach for identification and relative quantification of Trx target disulfides in complex protein extracts is described. The procedure utilizes the isotope-coded affinity tag (ICAT) reagents containing a thiol reactive iodoacetamide group and a biotin affinity tag to target peptides containing reduced cysteine residues. The identification of substrates for Trx and the extent of target disulfide reduction is determined by LC-MS/MS-based quantification of tryptic peptides labeled with {"}light{"} (12C) and {"}heavy{"} (13C) ICAT reagents. The methodology can be adapted to monitor the effect of different reductants or oxidants on the redox status of thiol/disulfide proteomes in biological systems.",
keywords = "Cysteine, Disulfide, Iodoacetamide, Isotope-coded affinity tag, Redox proteomics, Thiol, Thioredoxin",
author = "Per H{\"a}gglund and Jakob Bunkenborg and Kenji Maeda and Christine Finnie and Birte Svensson",
year = "2014",
doi = "10.1007/978-1-62703-631-3_47",
language = "English",
isbn = "9781627036306",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "677--685",
editor = "Jorrin-Novo, {Jesus V.}",
booktitle = "Plant Proteomics",
address = "United States",

}

RIS

TY - CHAP

T1 - Identification of thioredoxin target disulfides using isotope-coded affinity tags

AU - Hägglund, Per

AU - Bunkenborg, Jakob

AU - Maeda, Kenji

AU - Finnie, Christine

AU - Svensson, Birte

PY - 2014

Y1 - 2014

N2 - Thioredoxins (Trx) are small redox proteins that reduce disulfide bonds in various target proteins and maintain cellular thiol redox control. Here, a thiol-specific labeling and affinity enrichment approach for identification and relative quantification of Trx target disulfides in complex protein extracts is described. The procedure utilizes the isotope-coded affinity tag (ICAT) reagents containing a thiol reactive iodoacetamide group and a biotin affinity tag to target peptides containing reduced cysteine residues. The identification of substrates for Trx and the extent of target disulfide reduction is determined by LC-MS/MS-based quantification of tryptic peptides labeled with "light" (12C) and "heavy" (13C) ICAT reagents. The methodology can be adapted to monitor the effect of different reductants or oxidants on the redox status of thiol/disulfide proteomes in biological systems.

AB - Thioredoxins (Trx) are small redox proteins that reduce disulfide bonds in various target proteins and maintain cellular thiol redox control. Here, a thiol-specific labeling and affinity enrichment approach for identification and relative quantification of Trx target disulfides in complex protein extracts is described. The procedure utilizes the isotope-coded affinity tag (ICAT) reagents containing a thiol reactive iodoacetamide group and a biotin affinity tag to target peptides containing reduced cysteine residues. The identification of substrates for Trx and the extent of target disulfide reduction is determined by LC-MS/MS-based quantification of tryptic peptides labeled with "light" (12C) and "heavy" (13C) ICAT reagents. The methodology can be adapted to monitor the effect of different reductants or oxidants on the redox status of thiol/disulfide proteomes in biological systems.

KW - Cysteine

KW - Disulfide

KW - Iodoacetamide

KW - Isotope-coded affinity tag

KW - Redox proteomics

KW - Thiol

KW - Thioredoxin

U2 - 10.1007/978-1-62703-631-3_47

DO - 10.1007/978-1-62703-631-3_47

M3 - Book chapter

C2 - 24136556

AN - SCOPUS:84934443529

SN - 9781627036306

T3 - Methods in Molecular Biology

SP - 677

EP - 685

BT - Plant Proteomics

A2 - Jorrin-Novo, Jesus V.

PB - Humana Press

ER -

ID: 240157984