Purification of calmodulin from bovine parotid gland

Abstract

Calmodulin was purified from bovine parotid gland. This calmodulin showed a single band upon sodium dodecyl sulfate polyacrylamide gel electrophoresis, and a characteristic decrease of the mobility on native gel in the presence of Ca2+. The parotid gland calmodulin activated also calmodulin-deficient cyclic nucleotide phosphodiesterase in a Ca2+-dependent fashion, and this activation was abolished by trifluoperazine, W-7 or chlorpromazine. These results may indicate clearly the existence of calmodulin in bovine parotid gland.