scholarly journals The Effect of α-Tocopheryl Succinate on Succinate Respiration in Rat Liver Mitochondria

2015 ◽  
pp. S609-S615 ◽  
Author(s):  
O. SOBOTKA ◽  
Z. DRAHOTA ◽  
O. KUČERA ◽  
R. ENDLICHER ◽  
H. RAUCHOVÁ ◽  
...  
Keyword(s):  
Concentration Dependence ◽  
Rat Liver ◽  
Liver Homogenate ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Experimental Models ◽  
Rat Liver Mitochondria ◽  
Isolated Mitochondria ◽  
Significant Inhibitory Effect ◽  
Tocopheryl Succinate

We compared the effect of α-tocopheryl succinate (TOS) on succinate-dependent respiration in rat liver mitochondria, homogenate and permeabilized hepatocytes in both a coupled and uncoupled state. In isolated mitochondria, a significant inhibitory effect was observed at a concentration of 5 µM, in liver homogenate at 25 µM and in permeabilized hepatocytes at 50 µM. The inhibitory effect of TOS on succinate respiration in an uncoupled state was less pronounced than in a coupled state in all the experimental models tested. When the concentration dependence of the TOS inhibitory effect was tested, the most sensitive in both states were isolated mitochondria; the most resistant were permeabilized hepatocytes.

BIOCHEMICAL STUDIES ON TOFRANIL

1961 ◽  
Vol 39 (3) ◽  
pp. 551-558 ◽  
Author(s):  
P. N. Abadom ◽  
K. Ahmed ◽  
P. G. Scholefield
Keyword(s):  
Rat Brain ◽  
Rat Liver ◽  
Brain Cortex ◽  
Respiratory Activity ◽  
Liver Mitochondria ◽  
Brain Mitochondria ◽  
Inhibitory Effect ◽  
Rat Liver Mitochondria ◽  
Brain Cortex Slices ◽  
Cortex Slices

Tofranil inhibits the respiratory activity of rat brain cortex slices incubated in a glucose-containing medium. It also inhibits the uptake and incorporation of glycine-1-C14at concentrations which have only a slight inhibitory effect on the respiration of slices. Tofranil also inhibits oxidative phosphorylation in both rat liver and rat brain mitochondria but at higher concentrations respiration is greatly affected. Tofranil differs quantitatively from chlorpromazine in its greater inhibitory effect on the ATP–Pi32exchange reaction and its lesser effect on the cytochrome c oxidase activity of rat liver mitochondria.

scholarly journals Protein-mediated uptake of vitamin B12 by isolated mitochondria

Blood ◽  
1976 ◽  
Vol 47 (6) ◽  
pp. 923-930 ◽  
Author(s):  
RA Gams ◽  
EM Ryel ◽  
F Ostroy
Keyword(s):  
Vitamin B12 ◽  
Rat Liver ◽  
Mitochondrial Respiration ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Isolated Rat Liver ◽  
Isolated Mitochondria ◽  
Isolated Rat

Abstract Protein-mediated B12 uptake by isolated rat liver mitochondria has been shown to be enhanced by plasma transcobalamin (TC-II) but not by salivary R binder in vitro. The process is enhanced by calcium and depends on active mitochondrial respiration. Following uptake, cyanocobalamin is converted to adenosyl and methylcobalamins and released from the mitochondria. TC-II appears to be required for both cellular and mitochondrial uptake of vitamin B12.

Evidence for the Biosynthetic Difference between Isolated Mitochondria and Microsomes from Guinea-Pig and Rat Liver Regarding Lysophospharidic Acid, Phosphatidic Acid, CDP-Diglyceride, Phosphatidylglycerol, and Cardiolipin

1974 ◽  
Vol 52 (10) ◽  
pp. 936-939 ◽  
Author(s):  
J. B. Davidson ◽  
N. Z. Stanacev
Keyword(s):  
Guinea Pig ◽  
Phosphatidic Acid ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Marker Enzymes ◽  
Synthetic Enzymes ◽  
Isolated Mitochondria ◽  
Significant Difference ◽  
Nadph Cytochrome C Reductase

The enzymatic activities of marker enzymes (NADPH – cytochrome c reductase and glucose-6-phosphatase) and synthetic enzymes (acyl-CoA:sn-glycero-3-phosphate acyltransferase, CTP:sn-3-phosphatidic acid cytidyltransferase, and CDP-diglyceride:sn-glycero-3-phosphate phosphatidyltransferase) were measured in both isolated mitochondria and microsomes from liver of guinea pig and rat. Results thus obtained show a significant difference in activities of these enzymes between subcellular particles within species and between two examined species. The activity of acyl-CoA:glycero-3-phosphate acyltransferase in guinea-pig mitochondria parallels the activity of microsomal marker enzymes in this fraction, while in rat liver mitochondria the activity is relatively higher and cannot be accounted for by the microsomal content as determined by marker enzymes. Implications of these results regarding mitochondrial autonomy in the biosynthesis of polyglycero-phosphatides and their precursors are discussed.

scholarly journals Protein-mediated uptake of vitamin B12 by isolated mitochondria

Blood ◽  
1976 ◽  
Vol 47 (6) ◽  
pp. 923-930
Author(s):  
RA Gams ◽  
EM Ryel ◽  
F Ostroy
Keyword(s):  
Vitamin B12 ◽  
Rat Liver ◽  
Mitochondrial Respiration ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Isolated Rat Liver ◽  
Isolated Mitochondria ◽  
Isolated Rat

Protein-mediated B12 uptake by isolated rat liver mitochondria has been shown to be enhanced by plasma transcobalamin (TC-II) but not by salivary R binder in vitro. The process is enhanced by calcium and depends on active mitochondrial respiration. Following uptake, cyanocobalamin is converted to adenosyl and methylcobalamins and released from the mitochondria. TC-II appears to be required for both cellular and mitochondrial uptake of vitamin B12.

scholarly journals The inhibition of pyruvate and ls(+)-isocitrate oxidation by succinate oxidation in rat liver mitochondria

1969 ◽  
Vol 114 (3) ◽  
pp. 589-596 ◽  
Author(s):  
T. König ◽  
D. G. Nicholls ◽  
P. B. Garland
Keyword(s):  
Cytochrome B ◽  
Rat Liver ◽  
Rat Heart ◽  
Fold Increase ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
The Other ◽  
Rat Liver Mitochondria ◽  
Succinate Oxidation ◽  
Rapid Flow

1. The effects of succinate oxidation on pyruvate and also isocitrate oxidation by rat liver mitochondria were studied. 2. Succinate oxidation was without effect on pyruvate and isocitrate oxidation when respiration was maximally activated with ADP. 3. When respiration was partially inhibited by atractylate, succinate oxidation severely inhibited the oxidation of pyruvate and isocitrate. 4. This inhibitory effect of succinate was associated with a two- to three-fold increase in the reduction of mitochondrial NAD+ but no change in the reduction of cytochrome b. 5. It is concluded that, in the partially energy-controlled state, respiration is more severely inhibited at the first phosphorylating site than at the other two. 6. The effects of succinate oxidation are compared with those of palmitoylcarnitine oxidation. It is concluded that a rapid flow of electrons directly into the respiratory chain at the level of cytochrome b is in itself inadequate to inhibit the oxidation of intramitochondrial NADH. 7. The effects of succinate oxidation on pyruvate oxidation were similar in rat heart and liver mitochondria.

Binding of mitochondrial malate dehydrogenase to mitoplasts

1979 ◽  
Vol 57 (6) ◽  
pp. 662-665 ◽  
Author(s):  
Paula M. Strasberg ◽  
Keith A. Webster ◽  
Hasmukh V. Patel ◽  
Karl B. Freeman
Keyword(s):  
Malate Dehydrogenase ◽  
Rat Liver ◽  
Specific Binding ◽  
Liver Mitochondria ◽  
Scatchard Plot ◽  
Rat Liver Mitochondria ◽  
Isolated Mitochondria ◽  
Plot Analysis ◽  
Scatchard Plot Analysis ◽  
Mitochondrial Malate Dehydrogenase

The binding of 14C-labelled bovine and porcine malate dehydrogenase (EC 1.1.1.37) to rat liver mitochondria and mitoplasts was examined. The bovine enzyme was found to associate nonspecifically with isolated mitochondria and sonicated mitoplasts. Scatchard plot analysis suggested a specific binding to mitoplasts of the order of 5 pmol malate dehydrogenase per milligram of mitoplast protein. Porcine malate dehydrogenase dimer but not monomer exhibited a similar binding. The results are discussed in relation to the mechanism of uptake of the enzyme by mitochondria after synthesis on cytosolic ribosomes.

Experimental study on Reye's syndrome: Inhibitory effect of interferon alfa on acetylsalicylate-induced injury to rat liver mitochondria

Metabolism ◽  
1992 ◽  
Vol 41 (8) ◽  
pp. 887-892 ◽  
Author(s):  
Takashi Tomoda ◽  
Kohji Takeda ◽  
Takanobu Kurashige ◽  
Hideaki Enzan ◽  
Masanobu Miyahara
Keyword(s):  
Experimental Study ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Interferon Alfa ◽  
Rat Liver Mitochondria ◽  
Reye's Syndrome
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