Calmodulin-like activity in the soluble fraction of Escherichia coli

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Abstract

A heat-stable factor with properties similar to those of calmodulin was found in the fraction containing Ca2+-dependent cyclic AMP phosphodiesterase of Escherichiacoli. The factor activated such enzymes as cyclic nucleotide phosphodiesterase of bovine brain, (Ca2+,Mg2+)ATPase of human erythrocyte menbrane and myosin light chain kinase of rabbit myometrium in a Ca2+-dependent fashion with an apparent Ka of 5 × 10−5M. The factor and brain calmodulin had no effect on the phosphodiesterase of E.coli. It may be concluded that calmodulin or a calmodulin-like protein occurs in prokaryotes.

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Present address: The Department of Legal Medicine, Kumamoto University Medical School, Kumamoto 860, Japan

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On leave from the Department of Obstetricus and Gynecology, Kumamoto University Medical School, Kumamoto 860, Japan

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