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Optimizing the surf...
Optimizing the surface plasmon resonance/mass spectrometry interface for functional proteomics applications : How to avoid and utilize nonspecific adsorption
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- Larsericsdotter, Helén (författare)
- Mälardalens högskola
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- Jansson, Ö. (författare)
- Biacore AB, Uppsala, Sweden
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- Zhukov, A. (författare)
- Biacore AB, Uppsala, Sweden
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- Areskoug, D. (författare)
- Biacore AB, Uppsala, Sweden
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- Oscarsson, Sven (författare)
- Mälardalens högskola
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- Buijs, J. (författare)
- Biacore AB, Uppsala, Sweden
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(creator_code:org_t)
- Wiley, 2006
- 2006
- Engelska.
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Ingår i: Proteomics. - : Wiley. - 1615-9853 .- 1615-9861. ; 6:8, s. 2355-2364
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- 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
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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