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Iminodiacetic acid-modified magnetic poly(2-hydroxyethyl methacrylate)-based microspheres for phosphopeptide enrichment

    1.
    SYSNO ASEP0350470
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleIminodiacetic acid-modified magnetic poly(2-hydroxyethyl methacrylate)-based microspheres for phosphopeptide enrichment
    Author(s) Novotná, L. (CZ)
    Emmerová, T. (CZ)
    Horák, Daniel (UMCH-V) RID, ORCID
    Kučerová, Z. (CZ)
    Tichá, M. (CZ)
    Source TitleJournal of Chromatography A. - : Elsevier - ISSN 0021-9673
    Roč. 1217, č. 51 (2010), s. 8032-8040
    Number of pages9 s.
    Languageeng - English
    CountryNL - Netherlands
    KeywordsIMAC phosphopeptide separation ; IDA-modified magnetic microspheres ; Porcine pepsin A
    Subject RIVEE - Microbiology, Virology
    R&D ProjectsKAN401220801 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    GA203/09/0857 GA ČR - Czech Science Foundation (CSF)
    GAP503/10/0664 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z40500505 - UMCH-V (2005-2011)
    UT WOS000285429700014
    DOI10.1016/j.chroma.2010.08.058
    AnnotationMagnetic non-porous hydrophilic poly(2-hydroxyethyl methacrylate-co-glycidyl methacrylate) microspheres prepared by the dispersion polymerization and modified with iminodiacetic acid (IDA) were employed for the IMAC separation of phosphopeptides. Fe3+ and Ga3+ ions immobilized on IDA-modified magnetic microspheres were used for the enrichment of phosphopeptides from the proteolytic digests of two model proteins differing in their physico-chemical properties and phosphate group content: porcine pepsin A and bovine α-casein. The optimum conditions for phosphopeptide adsorption and desorption in both cases were investigated and compared. The phosphopeptides separated from the proteolytic digests were analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The ability of the prepared Fe3+- and Ga3+-IDA-modified magnetic microspheres to capture phosphopeptides from complex mixtures was shown on an example of bovine milk proteolytic digest.
    WorkplaceInstitute of Macromolecular Chemistry
    ContactEva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358
    Year of Publishing2011
Number of the records: 1  

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