Efficient and Specific Removal of Albumin from Human Serum Samples

Patient serum or plasma is frequently monitored for biochemical markers of disease or physiological status. Many of the rapidly evolving technologies of proteome analysis are being used to find additional clinically informative protein markers. The unusually high abundance of albumin in serum can in...

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Bibliographic Details
Published in:Molecular & cellular proteomics 2003-04, Vol.2 (4), p.262-270
Main Authors: Steel, Laura F, Trotter, Michael G, Nakajima, Pamela B, Mattu, Taj S, Gonye, Gregory, Block, Timothy
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antibodies, Monoclonal
Bacterial Proteins
Blood Protein Electrophoresis
Coloring Agents
Electrophoresis, Gel, Two-Dimensional
Humans
Immunoglobulin G - isolation & purification
Molecular Sequence Data
Peptide Mapping
Polymers
Proteomics
Serum
Serum Albumin - chemistry
Serum Albumin - immunology
Serum Albumin - isolation & purification
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Triazines
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Summary:Patient serum or plasma is frequently monitored for biochemical markers of disease or physiological status. Many of the rapidly evolving technologies of proteome analysis are being used to find additional clinically informative protein markers. The unusually high abundance of albumin in serum can interfere with the resolution and sensitivity of many proteome profiling techniques. We have used monoclonal antibodies against human serum albumin (HSA) to develop an immunoaffinity resin that is effective in the removal of both full-length HSA and many of the HSA fragments present in serum. This resin shows markedly better performance than dye-based resins in terms of both the efficiency and specificity of albumin removal. Immunoglobulins are another class of highly abundant serum protein. When protein G resin is used together with our immunoaffinity resin, Ig proteins and HSA can be removed in a single step. This strategy could be extended to the removal of any protein for which specific antibodies or affinity reagents are available.
ISSN:1535-9476
1535-9484
DOI:10.1074/mcp.M300026-MCP200