Identification of 3-Nitrotyosine-Modified Brain Proteins by Redox Proteomics

D. Allan Butterfield, Rukhsana Sultana

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

24 Scopus citations


Two-dimensional (2D) gel electrophoresis allows separation of complex mixtures of proteins based on isoelectric points and relative mobility. This method has not changed much fundamentally since their original description in the late 1970s. Despite several limitations, such as solubilization of membrane proteins and separation of highly basic proteins, this method has been used successfully in many laboratories as part of proteomics protocols. Our laboratory coupled 2D-PAGE with 2D Western blot analysis to identify brain proteins modified oxidatively with excess carbonylation, bound 4-hydroxy-2-nonenal, or 3-nitrotyrosine (3-NT) in various diseases and animal models of these disorders. This chapter describes in detail the protocol used for the identification of 3-NT-modified proteins in biological samples that may help in delineating the role of protein nitration in the progression or pathogenesis of various diseases.

Original languageEnglish
Title of host publicationNitric Oxide, Part F
EditorsEnrique Cadenas, Lester Packer
Number of pages14
StatePublished - 2008

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879

Bibliographical note

Funding Information:
This work was supported in part by NIH Grants AG‐05119 and AG‐10836.

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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