simple detection of phosphoproteins in sds-page by quercetin

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ID: 132377
2014
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Abstract
A novel fluorescence-based staining method was developed for phosphoprotein analysis in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Similar to the mechanism of immobilized metal ion affinity chromatography (IMAC), the method employed quercetin–aluminum (III)-appended complex as a fluoroprobe to selectively visualize phosphorylated proteins among total proteins. According to the results, as low as 16–32 ng of phosphoproteins (α-casein, β-casein and phosvitin) could be selectively detected in 90 min with a wide linear dynamic range. In addition, the specificity of this novel stain for phosphoproteins was confirmed by 1-D and 2-D SDS-PAGE, dephosphorylation, western blot and liquid chromatography–mass spectrometry analysis (LC–MS/MS), respectively.
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wang2014eupasimple Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
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Journal technological and economic development of economy
Year 2014
DOI
10.1016/j.euprot.2014.07.002
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