Identification of the NH2-terminal blocking group of calcineurin B as myristic acid.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001923:Brain Chemistry; D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D002148:Calmodulin-Binding Proteins; D002417:Cattle; D002849:Chromatography, Gas; D013058:Mass Spectrometry; D019814:Myristic Acid; D009227:Myristic Acids / Q000032:analysis*; D009419:Nerve Tissue Proteins / Q000302:isolation & purification*
D000596:Amino Acids; D002135:Calcium-Binding Proteins; D002148:Calmodulin-Binding Proteins; D009227:Myristic Acids; D009419:Nerve Tissue Proteins; D019814:Myristic Acid