Research Article

Virtual two-dimensional gel electrophoresis of high-density lipoproteins

  1. Rachel R. Ogorzalek Loo2,3,4,*,
  2. Lang Yam1,
  3. Joseph A. Loo1,2,3,4,
  4. Verne N. Schumaker1,3

Article first published online: 14 JUL 2004

DOI: 10.1002/elps.200405955

Issue

ELECTROPHORESIS

ELECTROPHORESIS

Special Issue: Paper Symposium BIOANALYSIS

Volume 25, Issue 14, pages 2384–2391, No. 14 July 2004

Additional Information

How to Cite

Ogorzalek Loo, R. R., Yam, L., Loo, J. A. and Schumaker, V. N. (2004), Virtual two-dimensional gel electrophoresis of high-density lipoproteins. ELECTROPHORESIS, 25: 2384–2391. doi: 10.1002/elps.200405955

Author Information

  1. 1

    Department of Chemistry and Biochemistry

  2. 2

    Department of Biological Chemistry

  3. 3

    Molecular Biology Institute

  4. 4

    UCLA-DOE Laboratory for Genomics and Proteomics, University of California, Los Angeles, CA, USA

*406 Paul D. Boyer Hall/MBI, 405 Hilgard Avenue, UCLA, Los Angeles, CA 90095, USA Fax: +11-310-206-7286

Publication History

  1. Issue published online: 14 JUL 2004
  2. Article first published online: 14 JUL 2004
  3. Manuscript Received: 2 FEB 2004

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Keywords:

  • High-density lipoproteins;
  • Matrix-assisted laser desorption/ionization-mass spectrometry;
  • Virtual two-dimensional gel electrophoresis

Abstract

High-density lipoproteins (HDLs) isolated by immunoaffinity chromatography and separated by immobilized pH gradient-isoelectric focusing (IPG-IEF) were examined by mass spectrometry directly, applying a new proteomics technology, virtual two-dimensional (2-D) gel electrophoresis. A preliminary examination of HDL particles has revealed at least 42 unique masses for protein species with isoelectric points between pH 5.47–5.04, some of which have not been observed previously. By delivering masses of intact proteins from complex cellular mixtures in a format that correlates directly to classical 2-D gel analyses, virtual 2-D gel electrophoresis constitutes a general discovery tool to expose and monitor protein isoforms and post-translational modifications. Furthermore, its general ability to deliver ions from sub-picomole level proteins enmeshed in complex cellular mixtures potentially fulfills the need of top-down proteomics to obtain intact protein ions from microscale samples. Additional comparison of such data to 2-D gel analyses and their identified proteins may elucidate the functions of the individual apolipoprotein components and the cardioprotective effects of HDL.

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