Identification of the NH2-terminal blocking group of calcineurin B as myristic acid

Andrew Aitken, P Cohen, S Santikarn, Dudley H Williams, Alexander Graham Calder, Alistair Smith, C B Klee

    Research output: Contribution to journalArticle

    171 Citations (Scopus)

    Abstract

    The NH2-terminal blocking group of the Ca2+-binding B-subunit of calcineurin (protein phosphatase-2B) has been identified as myristic acid by fast atom bombardment mass spectrometry and gas chromatography. The sequence, myristyl-Gly-Asn-Glu-Ala-, is very similar to that of the catalytic subunit of cyclic AMP-dependent protein kinase, the only other protein known to contain this fatty acid. This finding, and the elution of all myristyl peptides at 57% acetonitrile on reverse phase HPLC, may facilitate the identification of other proteins with this blocking group.
    Original languageEnglish
    Pages (from-to)314-318
    Number of pages5
    JournalFEBS Letters
    Volume150
    Issue number2
    DOIs
    Publication statusPublished - 27 Dec 1982

    Keywords

    • Amino Acids
    • Animals
    • Brain Chemistry
    • Calcium-Binding Proteins
    • Calmodulin-Binding Proteins
    • Cattle
    • Chromatography, Gas
    • Mass Spectrometry
    • Myristic Acid
    • Myristic Acids
    • Nerve Tissue Proteins
    • Protein phosphatase
    • Ca2+
    • Calmodulin
    • Mass spectrometry
    • Fatty acids
    • High-performance liquid High-performance liquid chromatography

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