Effect of ?-tocopherol and its derivatives on ATPase activity and oxidative phosphorylation in rat liver mitochondria

1987 ◽  
Vol 104 (3) ◽  
pp. 1224-1226
Author(s):  
I. Simidzhiev ◽  
V. E. Kagan ◽  
I. Minkov
Keyword(s):  
Oxidative Phosphorylation ◽  
Atpase Activity ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria

THE EFFECT OF RIBOFLAVIN DEFICIENCY AND GALACTOFLAVIN FEEDING ON OXIDATIVE PHOSPHORYLATION AND RELATED REACTIONS IN RAT LIVER MITOCHONDRIA

1961 ◽  
Vol 39 (1) ◽  
pp. 73-88 ◽  
Author(s):  
Robert E. Beyer ◽  
Stanley L. Lamberg ◽  
M. Arthur Neyman
Keyword(s):  
Electron Transport ◽  
Oxidative Phosphorylation ◽  
Energy Conservation ◽  
Atpase Activity ◽  
Exchange Rates ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Riboflavin Deficiency

The effect of riboflavin deficiency and feeding of galactoflavin on the flavin content of liver mitochondria, oxidative phosphorylation, Pi–ATP exchange, and ATPase activity was studied. Both dietary riboflavin deprivation and galactoflavin feeding resulted in a depressed flavin content of mitochondria, the latter treatment resulting in a more severe flavin loss. P/O ratios under all treatments were normal as were Pi–ATP exchange rates and the oxidation of succinate. Glutamate and β-hydroxybutyrate oxidations were depressed in mitochondria from rats fed galactoflavin for 15 or 28 days. DNP-activated ATPase was elevated in both flavin-deficient and galactoflavin-fed preparations while Mg++-activated ATPase was depressed in the galactoflavin-fed preparations. These results are discussed in relation to the hypothesis that flavin is involved in energy conservation in the diaphorase region of electron transport.

scholarly journals Oxidative phosphorylation. The specific binding of trimethyltin and triethyltin to rat liver mitochondria

1970 ◽  
Vol 118 (1) ◽  
pp. 171-179 ◽  
Author(s):  
W. N. Aldridge ◽  
B. W. Street
Keyword(s):  
Adipose Tissue ◽  
Oxidative Phosphorylation ◽  
Brown Adipose Tissue ◽  
Binding Site ◽  
Rat Liver ◽  
Specific Binding ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Affinity Constants ◽  
Brown Adipose

1. The binding of trimethyltin and triethyltin to rat liver mitochondria was determined and the results were analysed by the method of Scatchard (1949). 2. One binding site (site 1) has the correct characteristics for the site to which trimethyltin and triethyltin are attached when they inhibit oxidative phosphorylation. For each compound the concentration of site 1 is 0.8nmol/mg of protein and the ratios of their affinity constants are the same as the ratio of the concentrations inhibiting oxidative phosphorylation. 3. Binding site 1 is present in a fraction derived from mitochondria containing only 15% of the original protein. In this preparation ultrasonication rapidly destroyed site 1. 4. Dimethyltin and diethyltin do not prevent binding of triethyltin to rat liver mitochondria, whereas triethyl-lead does. 5. Trimethyltin and triethyltin bind to mitochondria from brown adipose tissue and the results indicate a binding site 1 similar to that in rat liver mitochondria. 6. The advantages and limitations of this approach to the study of inhibitors are discussed.

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