Large Scale Preparation of Calmodulin

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Abstract
A rapid large scale purification procedure based on three conventional purification steps, ammonium sulfate fractionation, DEAE cellulose and hydroxylapaptite chromotography yields gram amounts of calmodulin. The protein is more than 98% pure by SDS gel electrophoresis and amino acid composition. It is free of contaminating EGTA or EDTA and the omission of heat treatment or denaturing solvents during the preparat-ion avoids possible dena-turation of the protein and minimizes partial proteolysis.