Analysis of protein acylation.
File(s)
Author(s)
Zeidman, R
Jackson, CS
Magee, AI
Type
Journal Article
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.
Version
Accepted version
Date Issued
2009-02-28
Citation
Curr Protoc Protein Sci Vol.( Chapter 14 ) No.( ) pp Unit 14.2 - Unit 14.2
ISSN
1934-3663
Start Page
Unit 14.2
End Page
Unit 14.2
Copyright Statement
© 2009 by John Wiley & Sons, Inc. This is the post-peer-reviewed (but not final) version of the following article: Zeidman, R., Jackson, C.S., and Magee, A.I. 2009. Analysis of Protein Acylation. Curr. Protoc. Protein Sci. 55:14.2.1-14.2.12. © 2009 by John Wiley & Sons, Inc., which has been published in final form at http://www.mrw.interscience.wiley.com/emrw/9780471140863/cp/cpps/toc
Source Volume Number
Chapter 14