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KMID : 0383419690100010119
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Korean Modern Medical Journal
1969 Volume.10 No. 1 p.119 ~ p.129
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The effect of bovine serum albumin on the adenylate kinase activity and oxidative phosphorylation of rabbit liver mitochondria
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Abstract
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It has been known that the enzyme myokinase, or adenylate kinase, which catalyzes the establishment of an equilibrium among the three nucleotides, adenosine triphosphate, aenosine diphosphate, and adenylic acid, is localized in the mitochondria.
For the purpose of studying the effect of bovine serum albumin on the adenylate kinase activity and oxidative phosphorylation of rabbit liver mitochondria, the following experiments were undertaken:
1. Mitochondria were isolated from the rabbit liver with 0.25 M sucrose by the differential centrifugation technique of Schneider.
2. The method of paper chromatography and isotope exchange reaction between ^(14)C-AMP and ATP were used to determine the adenylate kinase activity of rabbit liver mitochondria after incubation of mitochondrial suspension with ^(14)G-AMP and ATP. These experiments have revealed the following results:
1. The adenylate kinase activity of liver mitochondria was activated by Mg^(++), this activation was augmented in the presence of bovine serum albumin.
2. The adenylate kinase activity of liver mitochondria was slightly activated by Ca^(++), this activation was inhibited by the addition of bovine serum albumin.
3. When the liver mitochondrial suspension including bovine serum albumin and Mg^(++) a, stored at 4℃ for 24 hours, its adenylate kinase activity was augmented markedly, however, in the stored Jiver mitochondrial suspension without bovine serum albumin, the inase activity was augmented to less extent.
4. Afeter heat treatment of liver mitochondria at 90℃ for 5 minutes, the andenylate kinase activity still survived.
5. In the liver raitochondrial suspension with bovine serum albumin, the adenylate kinase showed its maximum activity in a dilution 1 : 3 water, but in the suspension without bovine serum albumin the kinase showed its maximum acivity in a dilution 1 4 water.
6. The phosphorylation of liver mitochondria was inhibited by the addition of residual adenylate kinase, whereas oxygen consumption of liver mitochondria was not influenced by the residual adenylate kinase. Therefore, the oxidative phosphorylation of the liver mitochondria was reduced by the residual adenylate kinase. Bovine serum albumin protected the phosphorylation process of the liver mitochondria against residual adenylate kinase.
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