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Unrestricted analysis of modifications in proteins exposed to metal-catalyzed oxidation

ABSTRACT: Bovine serum albumin and human serum proteins subjected to metal ion-catalyzed oxidation were analysed by LC-MS followed by unrestricted "dependent peptide" data analysis focused on oxidative modifications

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human) Bos Taurus (bovine)

TISSUE(S): Blood Serum

SUBMITTER: Per Hägglund

LAB HEAD: Per Hägglund

PROVIDER: PXD006582 | Pride | 2017-09-21

REPOSITORIES: Pride

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			Action	DRS
	20160921_HomepackedPicofrit_K2_AB_MR_15cm_70min_BL1.raw	Raw
	20160921_HomepackedPicofrit_K2_AB_MR_15cm_70min_BL1_allPeptides.txt	Txt
	20160921_HomepackedPicofrit_K2_AB_MR_15cm_70min_BL2.raw	Raw
	20160921_HomepackedPicofrit_K2_AB_MR_15cm_70min_BL2_allPeptides.txt	Txt
	20160921_HomepackedPicofrit_K2_AB_MR_15cm_70min_BL3.raw	Raw

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Publications

Unrestricted Mass Spectrometric Data Analysis for Identification, Localization, and Quantification of Oxidative Protein Modifications.

Rykær Martin M Svensson Birte B Davies Michael J MJ Hägglund Per P

Journal of proteome research 20170929 11

Oxidation generates multiple diverse post-translational modifications resulting in changes in protein structure and function associated with a wide range of diseases. Of these modifications, carbonylations have often been used as hallmarks of oxidative damage. However, accumulating evidence supports the hypothesis that other oxidation products may be quantitatively more important under physiological conditions. To address this issue, we have developed a holistic mass spectrometry-based approach ...[more]

PMID: 28920440

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