Virtual two-dimensional gel electrophoresis of high-density lipoproteins
In: Electrophoresis; vol 25, iss 14, 2384-2391; 0173-0835; (2004)
Online
Elektronische Ressource
High-density lipoproteins (HDLs) isolated by immunoaffinity chromatography and separated by immobilized pH gradient-isoelectric focusing (IPG-IEF) were examined by mass spectrometry directly, applying a new proteomics technology, virtual two-dimensional (2-D) gel electrophoresis. A preliminary examination of HDL particles has revealed at least 42 unique masses for protein species with isoelectric points between pH 5.47-5.04, some of which have not been observed previously. By delivering masses of intact proteins from complex cellular mixtures in a format that correlates directly to classical 2-D gel analyses, virtual 2-D gel electrophoresis constitutes a general discovery tool to expose and monitor protein isoforms and post-translational modifications. Furthermore, its general ability to deliver ions from sub-picomole level proteins enmeshed in complex cellular mixtures potentially fulfills the need of top-down proteomics to obtain intact protein ions from microscale samples. Additional comparison of such data to 2-D gel analyses and their identified proteins may elucidate the functions of the individual apolipoprotein components and the cardioprotective effects of HDL.
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Virtual two-dimensional gel electrophoresis of high-density lipoproteins
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Autor/in / Beteiligte Person: | Ogorzalek Loo, Rachel R |
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Quelle: | Electrophoresis; vol 25, iss 14, 2384-2391; 0173-0835; (2004) |
Veröffentlichung: | 2004 |
Medientyp: | Elektronische Ressource |
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