Quantification of protein modification by oxidants

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Quantification of protein modification by oxidants. / Hawkins, Clare Louise; Morgan, Philip E; Davies, Michael Jonathan.

In: Free Radical Biology & Medicine, Vol. 46, No. 8, 15.04.2009, p. 965-88.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Hawkins, CL, Morgan, PE & Davies, MJ 2009, 'Quantification of protein modification by oxidants', Free Radical Biology & Medicine, vol. 46, no. 8, pp. 965-88. https://doi.org/10.1016/j.freeradbiomed.2009.01.007

APA

Hawkins, C. L., Morgan, P. E., & Davies, M. J. (2009). Quantification of protein modification by oxidants. Free Radical Biology & Medicine, 46(8), 965-88. https://doi.org/10.1016/j.freeradbiomed.2009.01.007

Vancouver

Hawkins CL, Morgan PE, Davies MJ. Quantification of protein modification by oxidants. Free Radical Biology & Medicine. 2009 Apr 15;46(8):965-88. https://doi.org/10.1016/j.freeradbiomed.2009.01.007

Author

Hawkins, Clare Louise ; Morgan, Philip E ; Davies, Michael Jonathan. / Quantification of protein modification by oxidants. In: Free Radical Biology & Medicine. 2009 ; Vol. 46, No. 8. pp. 965-88.

Bibtex

@article{5bcfc69b7cf04c6c8ec1a2a6217be687,
title = "Quantification of protein modification by oxidants",
abstract = "Proteins are major targets for oxidative damage due to their abundance and rapid rates of reaction with a wide range of radicals and excited state species, such as singlet oxygen. Exposure of proteins to these oxidants results in loss of the parent amino acid residue, formation of unstable intermediates, and the generation of stable products. Each of these events can be used, to a greater or lesser extent, to quantify damage to proteins. In this review the advantages and disadvantages of a number of these approaches are discussed, with an emphasis on methods that yield absolute quantitative data on the extent of protein modification. Detailed methods sheets are provided for many of these techniques.",
keywords = "Animals, Biochemistry, Biological Markers, Chromatography, High Pressure Liquid, Enzyme-Linked Immunosorbent Assay, Humans, Mass Spectrometry, Oxidants, Oxidation-Reduction, Oxidative Stress, Protein Processing, Post-Translational, Proteins, Reactive Oxygen Species, Spin Trapping, Statistics as Topic",
author = "Hawkins, {Clare Louise} and Morgan, {Philip E} and Davies, {Michael Jonathan}",
year = "2009",
month = "4",
day = "15",
doi = "10.1016/j.freeradbiomed.2009.01.007",
language = "English",
volume = "46",
pages = "965--88",
journal = "Free Radical Biology & Medicine",
issn = "0891-5849",
publisher = "Elsevier",
number = "8",

}

RIS

TY - JOUR

T1 - Quantification of protein modification by oxidants

AU - Hawkins, Clare Louise

AU - Morgan, Philip E

AU - Davies, Michael Jonathan

PY - 2009/4/15

Y1 - 2009/4/15

N2 - Proteins are major targets for oxidative damage due to their abundance and rapid rates of reaction with a wide range of radicals and excited state species, such as singlet oxygen. Exposure of proteins to these oxidants results in loss of the parent amino acid residue, formation of unstable intermediates, and the generation of stable products. Each of these events can be used, to a greater or lesser extent, to quantify damage to proteins. In this review the advantages and disadvantages of a number of these approaches are discussed, with an emphasis on methods that yield absolute quantitative data on the extent of protein modification. Detailed methods sheets are provided for many of these techniques.

AB - Proteins are major targets for oxidative damage due to their abundance and rapid rates of reaction with a wide range of radicals and excited state species, such as singlet oxygen. Exposure of proteins to these oxidants results in loss of the parent amino acid residue, formation of unstable intermediates, and the generation of stable products. Each of these events can be used, to a greater or lesser extent, to quantify damage to proteins. In this review the advantages and disadvantages of a number of these approaches are discussed, with an emphasis on methods that yield absolute quantitative data on the extent of protein modification. Detailed methods sheets are provided for many of these techniques.

KW - Animals

KW - Biochemistry

KW - Biological Markers

KW - Chromatography, High Pressure Liquid

KW - Enzyme-Linked Immunosorbent Assay

KW - Humans

KW - Mass Spectrometry

KW - Oxidants

KW - Oxidation-Reduction

KW - Oxidative Stress

KW - Protein Processing, Post-Translational

KW - Proteins

KW - Reactive Oxygen Species

KW - Spin Trapping

KW - Statistics as Topic

U2 - 10.1016/j.freeradbiomed.2009.01.007

DO - 10.1016/j.freeradbiomed.2009.01.007

M3 - Journal article

C2 - 19439229

VL - 46

SP - 965

EP - 988

JO - Free Radical Biology & Medicine

JF - Free Radical Biology & Medicine

SN - 0891-5849

IS - 8

ER -

ID: 129670374