Fructose diphosphatase from rabbit liver. II. Changes in catalytic properties induced by dinitrofluorobenzene.

In the preceding paper we have described the crystallization of fructose 1,6-diphosphatase from rabbit liver (1). The purified enzyme has been shown to be homogeneous in sucrose gradient centrifugation and in disk gel electrophoresis, and to catalyze the hydrolysis of fructose-l, 6-di-P and sedoheptulose-1,7-di-P at nearly equal rates (1, 2).