Unit

UNIT 14.2 Analysis of Protein Acylation

  1. Ruth Zeidman,
  2. Caroline S. Jackson,
  3. Anthony I. Magee

Published Online: 1 FEB 2009

DOI: 10.1002/0471140864.ps1402s55

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Zeidman, R., Jackson, C. S. and Magee, A. I. 2009. Analysis of Protein Acylation. Current Protocols in Protein Science. 55:14.2:14.2.1–14.2.12.

Author Information

  1. Molecular Medicine, National Heart & Lung Institute, Imperial College London, London, United Kingdom

Publication History

  1. Published Online: 1 FEB 2009
  2. Published Print: FEB 2009

Abstract

Proteins can be acylated with a variety of fatty acids attached by different covalent bonds, influencing, among other things, their function and intracellular localization. This unit describes methods to analyze protein acylation, both levels of acylation and also the identification of the fatty acid and the type of bond present in the protein of interest. Protocols are provided for metabolic labeling of proteins with tritiated fatty acids, for exploitation of the differential sensitivity to cleavage of different types of bonds, in order to distinguish between them, and for thin-layer chromatography to separate and identify the fatty acids associated with proteins. Curr. Protoc. Protein Sci. 55:14.2.1-14.2.12. © 2009 by John Wiley & Sons, Inc.

Keywords:

  • acylation;
  • palmitoylation;
  • myristoylation;
  • fatty acids;
  • protein modification