Kinetic behaviour of chicken liver mitochondrial malate dehydrogenase and lactate dehydrogenase mixtures |
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Affiliation: | 1. Department of Applied Biological Science, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan;2. Department of Chemistry, Tokyo Institute of Technology, 2-12-1 O-okayama, Meguro-ku, Tokyo 152-8551, Japan;1. Research and Development Unit, GYAH Corporation, Karaj, Iran;2. Department of Soil Science and Engineering, Faculty of Agriculture, Shahrekord University, P.O. Box 115, Shahrekord, Iran |
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Abstract: | ![]()
- 1.1. In the mitochondria of chicken liver cells there is lactate dehydrogenase activity that catalyses the reduction of the oxaloacetate by the NADH.
- 2.2. The presence of lactate dehydrogenase in the malate dehydrogenase preparations causes an apparent activation in the double-reciprocal plot at high oxaloacetate concentrations that depends on the lactate dehydrogenase/malate dehydrogenase ratio in the preparation.
- 3.3. The separation of the two molecular forms of chicken liver mitochondrial malate dehydrogenase, free from lactate dehydrogenase, is described.
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