Calmodulin-binding proteins of Tetrahymena microsomal membranes.
Tetrahymena calmodulin radioiodinated with a lactoperoxidase method retained full ability to activate Tetrahymena guanylate cyclase. Binding of [125I]calmodulin to Tetrahymena microsomal membranes was Ca2+-dependent and inhibited by excess unlabeled calmodulin or trifluoperazine. When Triton X-100-solubilized microsomes were chromatographed on calmodulin Sepharose, several proteins were found to interact with calmodulin in a Ca2+-dependent manner.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002147:Calmodulin / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism*; D007700:Kinetics; D008861:Microsomes / Q000378:metabolism*; D008970:Molecular Weight; D009994:Osmolar Concentration; D013769:Tetrahymena pyriformis / Q000378:metabolism*
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D002118:Calcium