[pH-induced inactivation of glycerol dehydrogenase from Bacillus megaterium]

The kinetic of the reversible dissociation of glycerol dehydrogenase from Bacillus megaterium in slightly alkaline medium was measured by biochemical, chemical and physical methods. The dissociation is followed by changes in the secondary structure and can be prevented by addition of NAD or increased potassium chloride concentration. Crosslinking by suberimidate, but not by monofunctional imido esters, shows a high stabilization against alkali, urea or heat inactivation caused by hindrance of dissociation.