Peptide Mapping and Purification of Phosphopeptides Using High-Performance Liquid Chromatography

Henning Juhl, Thomas R. Soderling

    Research output: Contribution to journalArticle

    11 Scopus citations

    Abstract

    This chapter describes peptide mapping and purification of phosphopeptides using high-performance liquid chromatography (HPLC). Protein phosphorylation is now firmly established as an important mechanism for regulation of diverse cellular functions, such as metabolism, membrane transport, muscle contraction, protein synthesis, neuronal activity, and cellular transformation by viruses. In addition, many phosphoproteins have multiple phosphorylation sites. One of the most complicated of these is skeletal muscle glycogen synthase, which contains at least seven phosphorylation sites per subunit. These multiple phosphorylations can be catalyzed by a number of different protein kinases. To establish the specificities of the kinases for the several phosphorylation sites, the HPLC methodology has been developed; this methodology is rapid and generally gives good recoveries of phosphopeptides.

    Original languageEnglish (US)
    Pages (from-to)37-48
    Number of pages12
    JournalMethods in Enzymology
    Volume99
    Issue numberC
    DOIs
    StatePublished - Jan 1 1983

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology

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