Sodium-23 nuclear magnetic resonance as an indicator of sodium binding to calmodulin and tryptic fragments, in relation to calcium content.
The relaxation rate enhancements of the 23Na nuclei for NaHCO3 solutions of calmodulin and its tryptic peptides TR-1 and TR-2 indicate true binding of Na+ ions to these biomolecules. With both TR-1 and TR-2, Na+ binding occurs in competition with Ca2+ and Mg2+ binding: log KNa approximately equal to 2, log KMg apoproximately equal to 4, log KCa approximately equal to 6 for TR-1; and log KNa approximately equal to 2, log KMg approximately equal to 3, log KCa approximately equal to 5 for TR-2. All the binding constants are systemically greater for binding  to TR-1, as compared to TR-2. There is also an increase in KNa for TR-1 of calmodulin as compared to the homologous tryptic fragment of troponin C. The increased binding is identified tentatively with site I of calmodulin. The binding constants KNa, KCa and KMg of calmodulin appear to be finely tuned to the intracellular concentrations of these cations.
D000818:Animals; D001665:Binding Sites; D001921:Brain; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D002417:Cattle; D007700:Kinetics; D008274:Magnesium; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments; D011485:Protein Binding; D012964:Sodium; D014357:Trypsin
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D010446:Peptide Fragments; D012964:Sodium; D014357:Trypsin; D008274:Magnesium