Abstract
Calmodulin has been isolated from uredospores of the bean rust fungus and purified to apparent homogeneity as judged using sodium dodecyl sulfatepolyacrylamide gels. The protein substituted for bovine calmodulin as an activator of Ca 2+-dependent cyclic nucleotide phosphodiesterase. Its molecular mass was 15.6 kDa in the presence of Ca 2+ and 17.0 kDa in its absence. Thep I was 4.4. The amino acid composition was generally similar to those of calmodulin from other fungi.
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