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 language | English |
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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
- 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