Semin Thromb Hemost 2004; 30(4): 485-489
DOI: 10.1055/s-2004-833483
Copyright © 2004 by Thieme Medical Publishers, Inc., 333 Seventh Avenue, New York, NY 10001, USA.

Analyzing the Platelet Proteome

Angel García1 , Nicole Zitzmann1 , Steve P. Watson2
  • 1Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom
  • 2Department of Pharmacology, University of Oxford, Oxford, United Kingdom
Further Information

Publication History

Publication Date:
08 September 2004 (online)

During the last 10 years, mass spectrometry (MS) has become a key tool for protein analysis and has underpinned the emerging field of proteomics. Using high-throughput tandem MS/MS following protein separation, it is potentially possible to analyze hundreds to thousands of proteins in a sample at a time. This technology can be used to analyze the protein content (i.e., the proteome) of any cell or tissue and complements the powerful field of genomics. The technology is particularly suitable for platelets because of the absence of a nucleus. Cellular proteins can be separated by either gel-based methods such as two-dimensional gel electrophoresis or one-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis followed by liquid chromatography (LC) -MS/MS or by multidimensional LC-MS/MS. Prefractionation techniques, such as subcellular fractionations or immunoprecipitations, can be used to improve the analysis. Each method has particular advantages and disadvantages. Proteomics can be used to compare the proteome of basal and diseased platelets, helping to reveal information on the molecular basis of the disease.

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 Dr.
Angel García-Alonso

Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford

South Parks Road

Oxford OX1 3QU, United Kingdom

Email: angel.garcia@bioch.ox.ac.uk