[Kinetics of chicken liver mitochondrial and cytoplasmic glutamate oxalacetate transaminase (author's transl)].
Electrophoresis at pH 7.4, on cellulose polyacetate strips, and specific staining, show the occurrence of two molecular forms of the mitochondrial and soluble isoenzymes from chicken liver aspartate aminotransferase. The optimum pH of the cytoplasmic enzyme with L-aspartate and alpha-ketoglutarate as substrats is approximately 7, while the mitochondrial one is practically unaffected in the interval 6-8. The kinetic reactional mechanism is of ping-pong bi-bi type for both enzymes, as confirmed by the method of Garces-Cleland, and their inhibitions by excess of the substrates L-aspartate and alpha-Ketoglutarate are competitive, in accordance with the proposed mechanism.
D000818:Animals; D001219:Aspartate Aminotransferases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000378:metabolism*; D001224:Aspartic Acid / Q000494:pharmacology; D002645:Chickens; D004588:Electrophoresis, Cellulose Acetate; D007656:Ketoglutaric Acids / Q000494:pharmacology; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000032:analysis / Q000378:metabolism; D008930:Mitochondria, Liver / Q000201:enzymology*; D012995:Solubility
D007656:Ketoglutaric Acids; D001224:Aspartic Acid; D008291:Malate Dehydrogenase; D001219:Aspartate Aminotransferases
Cinética de la glutamato oxalacetato transaminasa soluble y mitocondrial de hígado de pollo.