IMMUNOLOGICAL STUDIES OF LIVER KIDNEY AND MUSCLE FRUCTOSE 1,6-DIPHOSPHATASES

Immunological methods were employed to investigate possible structural relations between fructose 1,6-diphosphatases present in rabbit liver, kidney, and muscle. The liver and kidney enzymes were found to be immunologically identical, and distinct from the muscle enzyme. Liver and kidney fructose 1,6-diphosphatases were each inhibited approximately 80% by antiserum prepared against pure liver FDPase, whereas the activity of the muscle enzyme was not affected. In the Ouchterlony double-diffusion system liver and kidney FDPases gave a single continuous precipitin band of identity, and also behaved identically in immunoelectrophoresis. Muscle FDPase gave no precipitin bands in these tests and by activity stain was shown to have a different electrophoretic mobility. A method for the purification of rabbit kidney FDPase is described which yields a homogeneous preparation in high yield. © 1969.