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

FEBS Letters

Calder, A.Graham⁴  Klee, Claude B.¹  Williams, Dudley H.³  Santikarn, Sitthivet³  Smith, Alistair⁴  Aitken, Alastair²  Cohen, Philip² 

[1] National Cancer Institute, National Institutes of Health, Bethesda, MD 20205, USA;Dept of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland;University Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, England;Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB, Scotland

关键词: Protein phosphatase;    Ca2+;    Calmodulin;    Mass spectrometry;    Fatty acids;    High-performance liquid chromatography;   

DOI  :  10.1016/0014-5793(82)80759-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The NH₂-terminal blocking group of the Ca ²⁺-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.

【 授权许可】

Unknown