Purification of human epidermal calmodulin.

Human epidermal calmodulin was purified by phenothiazine-Sepharose affinity chromatography. The protein stimulated activator-deficient phosphodiesterase and was identified to be calmodulin by radioimmunoassay. Epidermal calmodulin demonstrated a Mr of 17,000 on gel permeation chromatography and migrated on sodium dodecyl sulfate-urea-polyacrylamide gel electrophoresis as a single band at the same location as rat testes calmodulin. The exact role of calmodulin in the epidermis remains to be defined.