Purification and biochemical characterization of calmodulin from Corylus avellana pollen

A calcium-binding protein identifiable as calmodulin has been isolated from Corylus avellana L. pollen by phenyl-sepharose chromatography and further purified by anion exchange fast protein liquid chromatography. This protein is recognized by a monoclonal antibody raised against pea calmodulin. It can activate bovine brain phosphodiesterase in a calcium dependent manner and shows a calcium dependent shift in electrophoretic mobility. 2-D gel electrophoresis reveals that the polypeptide is present as a single isoform in Corylus pollen. In addition the amino acid sequence of this protein is largely comparable to that of other known plant calmodulins and to bovine brain calmodulin.