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Efficient and specific removal of albumin from human serum samples
Journal article   Open access   Peer reviewed

Efficient and specific removal of albumin from human serum samples

Laura F Steel, Michael G Trotter, Pamela B Nakajima, Taj S Mattu, Gregory Gonye and Timothy Block
Molecular & cellular proteomics, v 2(4)
Apr 2003
PMID: 12754305
url
https://doi.org/10.1074/mcp.M300026-MCP200View
Published, Version of Record (VoR) Open

Abstract

Triazines Amino Acid Sequence Immunoglobulin G - isolation & purification Coloring Agents Humans Serum Albumin - isolation & purification Blood Protein Electrophoresis Molecular Sequence Data Electrophoresis, Gel, Two-Dimensional Antibodies, Monoclonal Bacterial Proteins Serum Albumin - immunology Peptide Mapping Proteomics Serum Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Polymers Serum Albumin - chemistry
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.

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Web of Science research areas
Biochemical Research Methods
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