| Aqueous polymer two-phase systems: effective tools for plasma membrane proteomics. | |
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MedLine Citation:
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PMID: 16972286 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Plasma membranes (PMs) are of particular importance for all living cells. They form a selectively permeable barrier to the environment. Many essential tasks of PMs are carried out by their proteinaceous components, including molecular transport, cell-cell interactions, and signal transduction. Due to the key role of these proteins for cellular function, they take center-stage in basic and applied research. A major problem towards in-depth identification and characterization of PM proteins by modern proteomic approaches is their low abundance and immense heterogeneity in different cells. Highly selective and efficient purification protocols are hence essential to any PM proteome analysis. An effective tool for preparative isolation of PMs is partitioning in aqueous polymer two-phase systems. In two-phase systems, membranes are separated according to differences in surface properties rather than size and density. Despite their rare application to the fractionation of animal tissues and cells, they represent an attractive alternative to conventional fractionation protocols. Here, we review the principles of partitioning using aqueous polymer two-phase systems and compare aqueous polymer two-phase systems with other methods currently used for the isolation of PMs. |
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Authors:
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Jens Schindler; Hans Gerd Nothwang |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
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Title: Proteomics Volume: 6 ISSN: 1615-9853 ISO Abbreviation: Proteomics Publication Date: 2006 Oct |
Date Detail:
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Created Date: 2006-10-23 Completed Date: 2007-01-17 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101092707 Medline TA: Proteomics Country: Germany |
Other Details:
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Languages: eng Pagination: 5409-17 Citation Subset: IM |
Affiliation:
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Abteilung Tierphysiologie, Fachbereich Biologie, Technische Universität Kaiserslautern, Kaiserslautern, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Biochemistry / methods Cell Membrane / metabolism* Humans Ligands Membrane Proteins / chemistry Polymers / chemistry* Proteome / chemistry* Proteomics / instrumentation*, methods* Salts / pharmacology Subcellular Fractions / metabolism Water / chemistry* |
| Chemical | |
Reg. No./Substance:
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0/Ligands; 0/Membrane Proteins; 0/Polymers; 0/Proteome; 0/Salts; 7732-18-5/Water |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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