Unit

UNIT 14.6 Analysis of Protein S-Nitrosylation

  1. Christopher M. Schonhoff1,
  2. Moran Benhar2

Published Online: 1 FEB 2011

DOI: 10.1002/0471140864.ps1406s63

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Schonhoff, C. M. and Benhar, M. 2011. Analysis of Protein S-Nitrosylation. Current Protocols in Protein Science. 63:14.6:14.6.1–14.6.21.

Author Information

  1. 1

    Tufts Cummings School of Veterinary Medicine, North Grafton, Massachusetts

  2. 2

    Technion-Israel Institute of Technology, Haifa, Israel

Publication History

  1. Published Online: 1 FEB 2011
  2. Published Print: FEB 2011

Abstract

S-Nitrosylation, the redox-based modification of cysteine thiol side chains by nitric oxide, is a dynamic and reversible post-translational modification of proteins that subserves many important cellular functions. Analysis of protein S-nitrosylation is often challenging due to methodological limitations and the effects of various chemical and physical parameters. Despite these technical challenges, a growing number of useful methods are now available to analyze protein S-nitrosylation. In this unit, several important methods to measure protein S-nitrosylation and denitrosylation are discussed and evaluated. Recommendations are given regarding the potential and the applicability of the methods discussed. Curr. Protoc. Protein Sci. 63:14.6.1-14.6.21. © 2011 by John Wiley & Sons, Inc.

Keywords:

  • nitric oxide;
  • S-nitrosylation;
  • Saville-Griess assay;
  • chemical reduction/chemiluminescence;
  • DAN assay;
  • biotin-switch method