Immobilized glutamate oxaloacetate transaminase. Steady state kinetic analysis and stability studies.
1. Glutamate oxaloacetate transaminase (L-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) was immobilized on amino ethyl cellulose using the bifunctional reagent diethyl adipimidate. 2. The steady state kinetic analysis was performed for the particulate and the free enzyme, and the Michaelis constants measured for the amino ethyl cellulose derivative were not greatly different from those measured for the free glutamate oxaloacetate transaminase, while the latter were in good agreement with values in the literature. 3. The amino ethyl cellulose-glutamate oxaloacetate transaminase was slightly more stable than the free enzyme at 65 degrees C, but was stabilised less by polyethylene glycol than the free enzyme.
D000272:Adipates; D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism*; D002482:Cellulose / Q000031:analogs & derivatives; D004355:Drug Stability; D006358:Hot Temperature; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology; D011092:Polyethylene Glycols / Q000494:pharmacology; D011485:Protein Binding; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D012995:Solubility; D013552:Swine
D000272:Adipates; D011092:Polyethylene Glycols; D011732:Pyridoxal Phosphate; D002482:Cellulose; D001219:Aspartate Aminotransferases