Characterization of the Ca2+ binding sites of calmodulin from bovine testis using 43Ca and 113Cd NMR.

The exchange rates of Ca2+ ions to the two classes of sites on calmodulin have been determined from the temperature dependence of the 43Ca NMR line width. The exchange rates were found to differ by a factor of about 40 at room temperature. The apparent pK value for one of these classes was estimated from the pH dependence of the 43Ca line width. The pK values of the two-high-affinity sites were found to differ about 0.1-1. Zn2+ ions were shown to bind to calmodulin and affect the exchange rates of Ca2+ and Cd2+ for all four sites.