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Optimizing the surface plasmon resonance/mass spectrometry interface for functional proteomics applications: How to avoid and utilize nonspecific adsorption
Mälardalen University.
Biacore AB, Uppsala, Sweden.
Biacore AB, Uppsala, Sweden.
Biacore AB, Uppsala, Sweden.
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2006 (English)In: Proteomics, ISSN 1615-9853, E-ISSN 1615-9861, Vol. 6, no 8, 2355-2364 p.Article in journal (Refereed) Published
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Abstract [en]

A great challenge in functional or interaction proteomics is to map protein networks and establish a functional relationship between expressed proteins and their effects on cellular processes. These cellular processes can be studied by characterizing binding partners to a "bait" protein against a complex background of other molecules present in cells, tissues, or biological fluids. This so-called ligand fishing process can be performed by combining surface plasmon resonance biosensors with MS. This combination generates a unique and automated method to quantify and characterize biomolecular interactions, and identify the interaction partners. A general problem in chip-based affinity separation systems is the large surface-to-volume ratio of the fluidic system. Extreme care, therefore, is required to avoid nonspecific adsorption, resulting in losses of the target protein and carry-over during the affinity purification process, which may lead to unwanted signals in the final MS analysis and a reduction in sensitivity. In this study, carry-over of protein and low-molecular weight substances has been investigated systematically and cleaning strategies are presented. Furthermore, it is demonstrated that by the introduction of colloidal particles as a capturing and transporting agent, the recovery yield of the affinity-purified ligand could be improved nearly twofold.

Place, publisher, year, edition, pages
2006. Vol. 6, no 8, 2355-2364 p.
Keyword [en]
Interactions, Mass spectrometry, Proteins, Surface plasmon resonance, adsorption, article, functional proteomics, instrumentation, matrix assisted laser desorption ionization time of flight mass spectrometry, priority journal, separation technique, technique, Animals, Biosensing Techniques, Cattle, Ligands, Protein Array Analysis, Proteomics, Reproducibility of Results, Serum Albumin
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URN: urn:nbn:se:mdh:diva-31904DOI: 10.1002/pmic.200401353Scopus ID: 2-s2.0-33646237111OAI: oai:DiVA.org:mdh-31904DiVA: diva2:937831
Available from: 2016-06-16 Created: 2016-06-14 Last updated: 2016-06-16Bibliographically approved

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CiteExportLink to record
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Citation style
  • apa
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  • de-DE
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