Diagonal gel electrophoretic analysis of protein disulfides: Principles and applications

Xiaoting Luo, Rongrong Li, Liang Jun Yan

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Protein cysteine residues are constantly undergoing redox modifications, and many of them are involved in disulfide formation. In this chapter, we first give an overview of the diagonal gel analysis method for the identification of protein disulfides followed by the application of the method for the identification of mitochondrial proteins that have endogenous disulfide bonds or form disulfide bonds upon oxidative stress. Data that show that the albumin precursor protein could be identified by this method, and that many proteins form disulfide bonds after treatment with diamide are presented. The data presented in this chapter indicate that this diagonal gel analytical method, when used in conjunction with mass spectrometric peptide sequencing, can provide a powerful tool for studying protein disulfide proteomics.

Original languageEnglish
Title of host publicationReactive Oxygen Species, Lipid Peroxidation and Protein Oxidation
PublisherNova Science Publishers, Inc.
Pages87-94
Number of pages8
ISBN (Electronic)9781634631921
ISBN (Print)9781633218864
StatePublished - 1 Oct 2014

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Keywords

  • Diagonal gel electrophoresis
  • Disulfides
  • Mass spectrometry
  • Mitochondria
  • Redox modifications

Cite this

Luo, X., Li, R., & Yan, L. J. (2014). Diagonal gel electrophoretic analysis of protein disulfides: Principles and applications. In Reactive Oxygen Species, Lipid Peroxidation and Protein Oxidation (pp. 87-94). Nova Science Publishers, Inc..