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-GlyAsnGluAla-, 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 language | English |
|---|---|
| Pages (from-to) | 314-318 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 150 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 27 Dec 1982 |
Keywords
- Ca
- Calmodulin
- Fatty acids
- High-performance liquid chromatography
- Mass spectrometry
- Protein phosphatase
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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