An ultracentrifuge study on the self-association of glucose dehydrogenase from Bacillus megaterium.
The self-association of glucose dehydrogenase (beta-D-glucose:NAD(P) 1-oxidoreductase, EC 1.1.1.47) from Bacillus megaterium was studied by analytical ultracentrifugation. The pH and composition of the buffer used were such that, owing to a reversible partial dissociation of the tetrameric enzyme, enzyme activity was reduced. It was found that under these conditions the protein exists in a monomer/dimer/tetramer association equilibrium.
D001410:Bacillus megaterium / Q000201:enzymology*; D002237:Carbohydrate Dehydrogenases; D055598:Chemical Phenomena; D002621:Chemistry; D042843:Glucose 1-Dehydrogenase; D005948:Glucose Dehydrogenases; D046911:Macromolecular Substances; D013997:Time Factors; D014461:Ultracentrifugation
D046911:Macromolecular Substances; D002237:Carbohydrate Dehydrogenases; D005948:Glucose Dehydrogenases; D042843:Glucose 1-Dehydrogenase