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J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.R900005-JLR200 on February 19, 2009

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Journal of Lipid Research, Vol. 50, 781-786, May 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Thematic Review

Thematic Review Series: Proteomics. Proteomic analysis of lipid-protein complexes

Tomas Vaisar1

Department of Medicine, University of Washington, Seattle, WA 98109

Published, JLR Papers in Press, February 19, 2009.

1 To whom correspondence should be addressed. e-mail: tvaisar{at}u.washington.edu

There is intense interest in comprehensive proteomic approaches for analyzing integral membrane proteins and lipoproteins. Key features of mass spectrometric analysis center on enriching biological material for proteins of interest, efficiently digesting them, extracting the resulting peptides, and using fractionation methods to comprehensively sample proteins or peptides by tandem mass spectrometry. However, lipid-associated proteins are generally rich in hydrophobic domains and are often low in abundance. These features, together with the associated lipid, make their mass spectrometric analysis technically challenging. In this article, we review analytical strategies for successful proteomic analysis of lipid-associated proteins.

Supplementary key words integral membrane proteins • lipoproteins • mass spectrometry

Abbreviations: apo, apolipoprotein; 2DE, two-dimensional electrophoresis; IDL, intermediate density lipoprotein; LC, liquid chromatography; MS, mass spectrometry; MS/MS, tandem mass spectrometry; SELDI, surface-enhanced laser desorption ionization


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J. Lipid Res., October 1, 2009; 50(10): 1967 - 1975.
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Copyright © 2009 by the American Society for Biochemistry and Molecular Biology.
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