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.
D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D002147:Calmodulin / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004817:Epidermis / Q000032:analysis*; D006801:Humans; D008970:Molecular Weight; D011863:Radioimmunoassay
D002135:Calcium-Binding Proteins; D002147:Calmodulin