Reversible association of ox liver glutamate dehydrogenase with the inner mitochondrial membrane.
A comparative study on the catalytic and allosteric properties of particulate and soluble forms of ox liver glutamate dehydrogenase has been carried out. The response of the bound enzyme to release by various effectors was investigated. The particulate enzyme was found to have catalytic activities similar to the free enzyme in contrast to its behaviour when bound to pure anionic phospholipids. Possible reasons for such outstanding differences are discussed.
D000494:Allosteric Regulation; D000818:Animals; D002384:Catalysis; D002417:Cattle; D004355:Drug Stability; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000201:enzymology; D007656:Ketoglutaric Acids / Q000378:metabolism; D008930:Mitochondria, Liver / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D009994:Osmolar Concentration; D013367:Submitochondrial Particles / Q000201:enzymology; D013816:Thermodynamics
D007656:Ketoglutaric Acids; D009243:NAD; D005969:Glutamate Dehydrogenase