Abstract
Chromatin associated proteins such as histone and protamine and myelin basic protein inhibit the activities of calmodulin-dependent cyclic nucleotide phosphodiesterase and myosin light chain kinase supported by Ca 2+ and calmodulin in a dose-dependent manner. The inhibition of these enzymes induced by the proteins is completely abolished by high concentration of calmodulin but not with that of Ca 2+. Kinetic analysis of this inhibition reveals that the proteins inhibit these enzyme activities in a competitive fashion with calmodulin. The proteins bind to calmodulin on a calmodulin coupled-agarose affinity column in the presence of Ca 2+. It is suggested that endogenous basic proteins interact with calmodulin and may modulate intracellular regulation by calmodulin.
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