Calmodulin binding to human spectrin.
Calmodulin is shown to interact with human spectrin dimer. The binding was highly calcium-dependent and observed in two different kinds of experiments. Firstly, affinity chromatography of calmodulin on a Sepharose 4B column with immobilized spectrin, and secondly, partition in aqueous two-phase polymer systems. In the column experiments stoichiometric amounts of calmodulin were retained on the spectrin-Sepharose column when micromolar concentrations of calcium were present. The calmodulin bound could be eluted with EGTA. The partition coefficient of calmodulin in an aqueous two-phase polymer system containing calcium was changed upon addition of spectrin, indicating an association between the two proteins. In the absence of calcium, spectrin did not cause any change in the partition behaviour of calmodulin, thus showing that the association requires calcium.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002147:Calmodulin / Q000378:metabolism*; D002417:Cattle; D002846:Chromatography, Affinity; D006801:Humans; D011108:Polymers; D011485:Protein Binding; D012995:Solubility; D012997:Solvents; D013049:Spectrin / Q000378:metabolism*
D002147:Calmodulin; D011108:Polymers; D012997:Solvents; D013049:Spectrin; D002118:Calcium