Efficient enrichment of intact phosphorylated proteins by modified immobilized metal-affinity chromatography

Phosphoproteome studies are hampered by the lack of methods which allow a comprehensive and fast analysis of intact phosphoproteins. Here we describe an immobilized metal‐affinity chromatography (IMAC)‐based technique for the enrichment of phosphorylated proteins, which allows recovery of up to 90%...

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Veröffentlicht in:	Proteomics (Weinheim) 2005-12, Vol.5 (18), p.4678-4683
Hauptverfasser:	Dubrovska, Anna, Souchelnytskyi, Serhiy
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biologi Biological and medical sciences Biology Cell and molecular biology Cell Line Cell- och molekylärbiologi Chromatography, Affinity - methods Electrophoresis, Gel, Two-Dimensional - methods Epithelial Cells - metabolism Fundamental and applied biological sciences. Psychology Humans Immobilized metal-affinity chromatography Mammary Glands, Human - cytology MEDICIN MEDICINE Metals - chemistry Miscellaneous NATURAL SCIENCES NATURVETENSKAP Phosphoproteins - isolation & purification Phosphoproteomics Phosphorylation Proteins Proteome - analysis Smad2 Protein - isolation & purification Two-dimensional gel electrophoresis
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Beschreibung
Zusammenfassung:	Phosphoproteome studies are hampered by the lack of methods which allow a comprehensive and fast analysis of intact phosphoproteins. Here we describe an immobilized metal‐affinity chromatography (IMAC)‐based technique for the enrichment of phosphorylated proteins, which allows recovery of up to 90% of phosphoproteins. This technique is compatible with 2‐DE and can be applied to cultured cells and tissues.
ISSN:	1615-9853 1615-9861 1615-9861
DOI:	10.1002/pmic.200500002