Proteomics

Dataset Information

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Oxidized fibrinogen HPLC-MS/MS


ABSTRACT: Fibrinogen is highly susceptible to oxidation compared to other plasma proteins. Fibrinogen oxidation damages its structure and affects the protein function. Fibrinogen was isolated from citrated human plasma by the modified cold ethanol precipitation technique. Oxidation of fibrinogen by ozone: a solution of 2.0 mg of fibrinogen in 1 ml of 0.05 M Tris/0.15 M NaCl buffer (pH 7.4) was introduced into a quartz reactor filled with ozone–oxygen mixture. The full exhaustion of ozone in each experiment was confirmed by spectrophotometry by the absorption band at 254 nm. The amount of ozone was varied in the range of 50–100 μM per 1 μM of fibrinogen. Ozone-induced oxidative modifications of the fibrinogen Aα, Bβ, and γ polypeptide chains upon addition of various amounts of the oxidizer have been studied by mass-spectrometry.

INSTRUMENT(S): LTQ FT Ultra

ORGANISM(S): Homo sapiens  

TISSUE(S): Blood Plasma

DISEASE(S): Not Available

SUBMITTER: Lyubov Yurina  

LAB HEAD: Mark Rosenfeld

PROVIDER: PXD012046 | Pride | 2019-04-04

REPOSITORIES: Pride

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Publications

Ozone-induced damage of fibrinogen molecules: identification of oxidation sites by high-resolution mass spectrometry.

Yurina Lyubov L   Vasilyeva Alexandra A   Indeykina Maria M   Bugrova Anna A   Biryukova Marina M   Kononikhin Alexey A   Nikolaev Evgene E   Rosenfeld Mark M  

Free radical research 20190523


Fibrinogen is highly susceptible to oxidation compared to other plasma proteins. Fibrinogen oxidation damages its structure and affects the protein function. Ozone-induced oxidative modifications of the fibrinogen Aα, Bβ, and γ polypeptide chains upon addition of various amounts of the oxidiser were studied by mass spectrometry. Amino acid residues located on all three chains and main structural parts of the protein were revealed to be involved in oxidation. The αC-connector was shown to be most  ...[more]

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