Calcium, calmodulin‐dependent protein phosphorylation in <i>Neurospora crassa</i>

Abstract

A calcium, calmodulin‐dependent protein kinase activity has been partially purified by calmodulin‐Sepharose affinity chromatography from the soluble fraction of Neurospora crassa . The phosphorylated peptide has an apparent molecular mass on SDS‐polyacrylamide gel of 47 kDa. The apparent half maximal phosphorylation is obtained after 1.5 min at 30° C in the presence of calcium and calmodulin. The apparent half maximal activation of the phosphorylation is obtained at 1 μM calcium, and 0.1 or 0.2 μM calmodulin from bovine brain or Neurospora , respectively. The 32 P incorporation is enhanced about 10‐fold by calmodulin.