A rapid, economical, and reproducible method for human serum delipidation and albumin and IgG removal for proteomic analysis

Methods Mol Biol. 2007:357:365-71. doi: 10.1385/1-59745-214-9:365.

Abstract

Serum is a readily available source for diagnostic assays, but the identification of disease-specific serum biomarkers has been impeded by the dominance of human serum albumin (HSA) and immunoglobulin G (IgG) in the serum proteome. Therefore, in order to observe lower-abundance serum proteins, removal or depletion of at least these two proteins is required. However, the depletion method needs to be inexpensive and reproducible. We describe such a protocol that combines delipidation by centrifugation, IgG removal with Protein G Sepharose, and HSA depletion with sodium chloride/ethanol precipitation. The protocol is streamlined to increase reproducibility and is compatible with many proteomic platforms, including two-dimensional gel electrophoresis, and high-performance liquid chromatography either offline or coupled online with a mass spectrometer. The reproducible depletion of lipids, IgG, and HSA permits a higher load of the remaining serum proteins, facilitating the identification of disease biomarkers.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomarkers / blood
  • Blood Protein Electrophoresis
  • Blood Proteins / analysis*
  • Blood Proteins / isolation & purification
  • Chromatography, Affinity
  • Female
  • Humans
  • Immunoglobulin G / blood
  • Immunoglobulin G / isolation & purification*
  • Lipids / blood
  • Lipids / isolation & purification
  • Male
  • Proteomics / methods*
  • Reproducibility of Results
  • Serum Albumin / isolation & purification*

Substances

  • Biomarkers
  • Blood Proteins
  • Immunoglobulin G
  • Lipids
  • Serum Albumin