Calmodulin‐Binding Proteins and Calcium/Calmodulin Regulated Enzyme Activities Associated with Brain Actomyosin

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Abstract
Calcium- and calmodulin-regulated ATPase and protein kinase activities are shown to be strongly associated with brain actomyosin. Similar enzymatic activities and an invariable polypeptide profile on sodium dodecyl sulfate-polyacrylamide gel electrophoresis were obtained for brain actomyosin taken through a solubilization-precipitation cycle (1.0-0.1 M KCl), or precipitated from buffers containing 1% Triton X-100 or 10 mM EDTA and 10 mM EGTA. These data suggest a specific complex of brain actomyosin with a protein kinase similar to calmodulin-dependent kinase II, a 190-kDa calmodulin-binding protein (P190), and a calmodulin-like polypeptide. P190 was the major substrate for endogenous calcium-dependent phosphorylation. 125I-Calmodulin overlay technique revealed four major calmodulin-binding polypeptides associated with brain actomyosin: 50- and 60-kDa subunits of the calmodulin-dependent kinase II, P19), and a high molecular weight polypeptide which is probably fodrin. A fraction enriched in P190 had Ca2+- and calmodulin-stimulated MgATPase activity, but not myosin-like K-EDTA ATPase activity. The lack of immunological cross reactivity between brain myosin heavy chain and P190 confirmed that they are distinct molecules.

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