Abstract
Methods for the resolution of glutamic acid decarboxylase of sunflower cotyledons into the apo- and co-enzyme moieties are described. The apoenzyme can be separated from codecarboxylase by repeated acid – ammonium sulphate treatment with about 90% resolution and 40–50% inactivation. A codecarboxylase factor can be isolated as the barium salt following denaturation and precipitation of the protein by trichloracetic acid.