Mitochondrial and supernatant glutamate-oxalacetate transaminases (EC 2.6.1.1) and supernatant glutamate-pyruvate transaminase (EC 2.6.1.2) were purified 89, 204 and 240-fold respectively, from dolphin muscle. Starch gel electrophoresis of crude and purified perparations revealed that all three enzymes exist as single forms. Km values of a-ketoglutarate, alanine, pyruvate and glutamate for the glutamate-pyruvate transaminase were 0.45, 8.2, 0.87 and 15 mM, respectively. For the glutamate-oxalacetate transaminases, the Km values of a-ketoglutarate, aspartate, oxalacetate and glutamate were 0.76, 0.50, 0.10 and 9.4 mM, respectively, for the mitochondrial form and 0.13, 2.4, 0.06 and 3.2 mM, respectively, for the supernatant form. In all cases, as the assay pH was decreased from pH 7.3, the Km values of the a-keto acids decreased while those of the amino acids increased. This caused the apparent equilibrium constants for the glutamate-oxalacetate transaminases to remain independent of pH. These values were 9.2 and 6.8 for the mitochondrial and supernatant forms, respectively where K'eq = [asPartate][α-ketoglutarate]/[glutamate][oxalacetate]. Studies of the inhibition of the glutamate-oxalacetate transaminases by dicarboxylic acids indicated that these enzymes may be controlled by pools of metabolic intermediates. Three key roles are suggested for the transminases in the energy metabolism of the diving mammal. First, it is believed that a combined action of the transaminases could enhance energy production during hypoxia by providing (1) fumarate from aspartate for the ATP producing reversal of succinate dehydrogenase and (2) α-ketoglutarate from glutamate for the GTP producing succinyl thiokinase reaction. Next, diving mammals probably accumulate more NADH than other mammals during hypoxia. The glutamate-oxalacetate transaminases seem particularly well suited for restoring redox
balance via the malate-aspartate cycle after aerobic metabolism is resumed. Finally, since migrating divers oxidize large amounts of stored fats, the combined reactions of the transaminases could be instrumental in providing increased supplies of oxalacetate to condense with the fat derived acetyl CoA in the citrate synthase reaction. / Science, Faculty of / Zoology, Department of / Graduate
| Identifer | oai:union.ndltd.org:UBC/oai:circle.library.ubc.ca:2429/19519 |
| Date | January 1974 |
| Creators | Owen, Terrance George |
| Source Sets | University of British Columbia |
| Language | English |
| Detected Language | English |
| Type | Text, Thesis/Dissertation |
| Rights | For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use. |
Page generated in 0.0017 seconds