HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: M300026-MCP200v1 2/4/262    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Steel, L. F. Articles by Block, T. Search for Related Content PubMed PubMed Citation Articles by Steel, L. F. Articles by Block, T. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 2:262-270, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

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

Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Jefferson Center for Biomedical Research, Doylestown, Pennsylvania 18901
^¶ Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111
^|| Isis Innovation, Ewert House, Ewert Place, Summertown, Oxford OX2 7SG, United Kingdom
^** Daniel Baugh Institute for Functional Genomics/Computational Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107

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.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				N. Seam, D. A. Gonzales, S. J. Kern, G. L. Hortin, G. T. Hoehn, and A. F. Suffredini Quality Control of Serum Albumin Depletion for Proteomic Analysis Clin. Chem., November 1, 2007; 53(11): 1915 - 1920. [Abstract] [Full Text] [PDF]

				J. Harezlak, M. Wang, D. Christiani, and X. Lin Quantitative quality-assessment techniques to compare fractionation and depletion methods in SELDI-TOF mass spectrometry experiments Bioinformatics, September 15, 2007; 23(18): 2441 - 2448. [Abstract] [Full Text] [PDF]

				F. W. Khwaja, J. S. Duke-Cohan, D. J. Brat, and E. G. Van Meir Attractin Is Elevated in the Cerebrospinal Fluid of Patients with Malignant Astrocytoma and Mediates Glioma Cell Migration. Clin. Cancer Res., November 1, 2006; 12(21): 6331 - 6336. [Abstract] [Full Text] [PDF]

				J.-B. Vincourt, F. Lionneton, G. Kratassiouk, F. Guillemin, P. Netter, D. Mainard, and J. Magdalou Establishment of a Reliable Method for Direct Proteome Characterization of Human Articular Cartilage Mol. Cell. Proteomics, October 1, 2006; 5(10): 1984 - 1995. [Abstract] [Full Text] [PDF]