Publikace detail

Comparison of methods for specific isolation of phosphopeptides by Immobilized Metal Ion Affinity Chromatography (IMAC)

Autoři: Kroupa Tomáš | Jankovičová Barbora | Bílková Zuzana | Hernychová Lenka

Rok: 2010

Druh publikace: ostatní - přednáška nebo poster

Strana od-do: nestránkováno

Tituly:

Jazyk	Název	Abstrakt	Klíčová slova
eng	Comparison of methods for specific isolation of phosphopeptides by Immobilized Metal Ion Affinity Chromatography (IMAC)	Protein phosphorylation is one of the most frequent post-translational modifications which plays role in cellular processes. The identification of phosphoproteins and the characterization of their phosphorylation sites are necessary for understanding of their biological roles. However, phosphopeptides are suppressed by non-phosphorylated ones during MS ionization. Thus, sensitive detection methods combining with selective isolation or enrichment of phosphorylated peptides/proteins are required. In this context IMAC is one of the strategies how obtain phosphorylated peptides for next analysis. The model Phosphopeptide Standard Mixture (INVITROGEN), digested α- and β-casein has been applied for selective enrichment of phosphopeptides. We compared commercially available IMAC particles such as IDA magnetic particles (Chemicell), Profinity™ IMAC resin (Bio-Rad) and PHOS-Select™ Iron Affinity Gel (Sigma Aldrich). Parameters such selectivity, required instrumentation and time-consumption were evaluated.	Comparison; isolation; phosphopeptides; Immobilized; Metal; Ion; Affinity; Chromatography

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