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 journalArticlepeer-review

181 Citations (Scopus)


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
Issue number2
Publication statusPublished - 27 Dec 1982


  • 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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