Abstract
The amino acid sequence of calmodulin which can be extracted from rabbit skeletal muscle with low ionic strength buffer and presumably activates myosin light chain kinase has been determined. It is a single polypeptide chain of 148 residues with a blocked N terminus. The sequence of the N terminal tripeptide and residues 98 and 99 were not determined unequivocally nor were the amide assignments of residues 48, 50, 58 and 60. The protein is otherwise identical with the subunit of phosphorylase kinase and bovine uterus calmodulin and very similar to all other mammalian calmodulins.
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