ALLOSTERIC PROPERTIES OF GLUTAMATE DEHYDROGENASES FROM DIFFERENT SOURCES.
The structure and allosteric properties of glutamate dehydrogenases from different sources have been studied by immunologic means. Despite structural differences detected by electrophoretic mobility and antigenicity, all the vertebrate enzymes responded similarly to allosteric modification. Bacterial glutamate dehydrogenase was immunologically unrelated to the vertebrate enzymes and did not respond to allosteric regulation.
D000818:Animals; D001717:Birds; D002417:Cattle; D005969:Glutamate Dehydrogenase; D006168:Guinea Pigs; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D051379:Mice; D011817:Rabbits; D051381:Rats; D012106:Research; D012756:Sheep; D034561:Sheep, Domestic; D013552:Swine
D005969:Glutamate Dehydrogenase
BIRDS; CATTLE; EXPERIMENTAL LAB STUDY; GEL DIFFUSION TESTS; GLUTAMATE DEHYDROGENASE; GUINEA PIGS; IMMUNOELECTROPHORESIS; MICE; RABBITS; RATS; SHEEP; SWINE