Solubilization and properties of the structurally-bound glucose dehydrogenase of Bacterium anitratum

Abstract

Abstract The cytochrome-linked glucose dehydrogenase of Bacterium anitratum was solubilized by protamine sulfate and ammonium sulfate in the presence of deoxycholate, and further purified on DEAE-cellulose and CM-cellulose. The enzyme behaved in these purification steps in the same way as the soluble glucose dehydrogenase present in the same organism. Further evidence for their identity was found in the presence in the solubilized enzyme of the 337-mμ absorption band that is a characteristic of the originally soluble enzyme, and in identical substrate specificity.