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PMID: 7758583 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Peroxynitrite-mediated oxidative protein modifications.

FEBS letters ·Vol. 364 ·No. 3 ·1995-05-15 ·Pages 279-82

Ischiropoulos H, al-Mehdi AB

Abstract

Proteins are targets of reactive species and detection of oxidatively modified proteins is often used as an index of oxidative stress. Peroxynitrite is a strong oxidant formed by reaction of nitric oxide with superoxide. Using fatty acid-free bovine serum albumin as a model we examined peroxynitrite-mediated protein modifications. The reaction of protein with peroxynitrite resulted in the oxidation of tryptophan and cysteine, in the nitration of tyrosine, in the formation of dityrosine, in the production of 2,4 dinitrophenylhydrazine-reactive carbonyls and in protein fragmentation. The formation of 3-nitrotyrosine represents a specific peroxynitrite-mediated protein modification that is different from modifications mediated by reactive oxygen species.

MeSH Terms
Animals Cysteine/chemistry Electrophoresis, Polyacrylamide Gel Fluorescence Hydrogen-Ion Concentration Male Nitrates/chemistry Oxidation-Reduction Oxidative Stress Phenylhydrazines/chemistry Rats Rats, Sprague-Dawley Serum Albumin, Bovine/chemistry Tryptophan/chemistry Tyrosine/analogs & derivatives,chemistry
Chemicals
Nitrates Phenylhydrazines 2,4-dinitrophenylhydrazine peroxynitric acid Serum Albumin, Bovine 3-nitrotyrosine Tyrosine Tryptophan Cysteine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ischiropoulos H
Institute for Environmental Medicine, University of Pennsylvania, School of Medicine, Philadelphia 19104, USA.
al-Mehdi A B
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1995-05-15
Pages
279-82
Language
English
Region
England
NLM ID
0155157
Subset
IM
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