Effects of protamine and strophanthin on mitochondrial potassium, sodium and water

1960 ◽  
Vol 199 (4) ◽  
pp. 653-656
Author(s):  
Leonard Share
Keyword(s):  
Rat Liver ◽  
Sodium Concentration ◽  
Water Metabolism ◽  
Intact Cells ◽  
Kidney Mitochondria ◽  
Potassium Sodium ◽  
Isolated Mitochondria ◽  
Liver And Kidney ◽  
Uncoupling Of Oxidative Phosphorylation ◽  
High Concentrations

A study was made of the effects of certain agents, which inhibit potassium transport in intact cells, on the potassium, sodium and water metabolism of isolated mitochondria. Protamine (4 mg/100 ml) induced swelling in rat liver and kidney mitochondria and impaired the ability of these mitochondria to concentrate potassium. These actions appeared to be associated with the uncoupling of oxidative phosphorylation. Protamine was without effect on the mitochondrial sodium concentration. Strophanthin at extremely high concentrations (1 gm/100 ml) was also found to induce swelling of rat liver, kidney and heart mitochondria and to interfere with the ability of the mitochondria to concentrate potassium. There was a tendency for mitochondrial sodium concentration to be elevated. It is concluded that the actions of protamine and strophanthin on mitochondria are qualitatively and quantitatively different from the actions of these substances on intact cells and that there are basic differences between the potassium concentrating mechanisms in mitochondria and in intact cells.

Depletion and Reaccumulation of Mitochondrial Sodium and Potassium: Effect of Adrenalectomy

1958 ◽  
Vol 194 (1) ◽  
pp. 47-52 ◽  
Author(s):  
Leonard Share
Keyword(s):  
Rat Liver ◽  
Potassium Concentration ◽  
Tap Water ◽  
Sodium Concentration ◽  
Sodium Depletion ◽  
Adrenocortical Insufficiency ◽  
Kidney Mitochondria ◽  
Potassium Effect ◽  
Liver And Kidney ◽  
Sodium And Potassium

The effect of 6–7 days of adrenocortical insufficiency (tap water and no steroids) on the movements of sodium and potassium in rat liver and kidney mitochondria was studied. Rat liver and kidney mitochondria were depleted of sodium or potassium. The ability of these particulates to accumulate sodium or potassium upon the addition of the particular ion to the incubation medium was determined. Adrenalectomy was without effect on the following: the rate of depletion of or the ability to reaccumulate sodium or potassium, the mitochondrial water content or the intramitochondrial potassium concentration. However, adrenalectomy did result in a consistently higher sodium concentration in kidney mitochondria in the sodium depletion-reaccumulation experiments.

Purification and Properties of α-Aminoadipate Aminotransferase from Rat Liver and Kidney Mitochondria

1991 ◽  
Vol 21 (2-3) ◽  
pp. 151-162 ◽  
Author(s):  
Madhumalti R. Mawal ◽  
Arindam Mukhopadhyay ◽  
Devendra R. Deshmukh
Keyword(s):  
Rat Liver ◽  
Kidney Mitochondria ◽  
Purification And Properties ◽  
Liver And Kidney

scholarly journals Two forms of aspartate aminotransferase in rat liver and kidney mitochondria

1968 ◽  
Vol 108 (4) ◽  
pp. 619-624 ◽  
Author(s):  
M. M. Bhargava ◽  
A. Sreenivasan
Keyword(s):  
Rat Liver ◽  
Aspartate Aminotransferase ◽  
High Speed ◽  
Rat Kidney ◽  
Liver Mitochondria ◽  
Supernatant Fraction ◽  
Rat Liver Mitochondria ◽  
Aminotransferase Activity ◽  
Kidney Mitochondria ◽  
Liver And Kidney

1. Butan-1-ol solubilizes that portion of rat liver mitochondrial aspartate aminotransferase (EC 2.6.1.1) that cannot be solubilized by ultrasonics and other treatments. 2. A difference in electrophoretic mobilities, chromatographic behaviour and solubility characteristics between the enzymes solubilized by ultrasonic treatment and by butan-1-ol was observed, suggesting the occurrence of two forms of this enzyme in rat liver mitochondria. 3. Half the aspartate aminotransferase activity of rat kidney homogenate was present in a high-speed supernatant fraction, the remainder being in the mitochondria. 4. A considerable increase in aspartate aminotransferase activity was observed when kidney mitochondrial suspensions were treated with ultrasonics or detergents. 5. All the activity after maximum activation was recoverable in the supernatant after centrifugation at 105000g for 1hr. 6. The electrophoretic mobility of the kidney mitochondrial enzyme was cathodic and that of the supernatant enzyme anodic. 7. Cortisone administration increased the activities of both mitochondrial and supernatant aspartate aminotransferases of liver, but only that of the supernatant enzyme of kidney.

scholarly journals The uptake of oxalate by rat liver and kidney mitochondria.

1986 ◽  
Vol 261 (26) ◽  
pp. 12197-12201
Author(s):  
T Strzelecki ◽  
M Menon
Keyword(s):  
Rat Liver ◽  
Kidney Mitochondria ◽  
Liver And Kidney

Effects of D-amino acids on lipoperoxidation in rat liver and kidney mitochondria

Amino Acids ◽  
2006 ◽  
Vol 32 (1) ◽  
pp. 31-37 ◽  
Author(s):  
C. Cortés-Rojo ◽  
M. Clemente-Guerrero ◽  
A. Saavedra-Molina
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Kidney Mitochondria ◽  
Liver And Kidney

scholarly journals The effects of acetylcolletotrichin on the mitochondrial respiratory chain

1974 ◽  
Vol 138 (3) ◽  
pp. 415-423 ◽  
Author(s):  
Bernard Foucher ◽  
J. B. Chappell ◽  
J. D. McGivan
Keyword(s):  
Mitochondrial Respiratory Chain ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Oxidative Activity ◽  
Detectable Effect ◽  
Succinate Oxidation ◽  
Kidney Mitochondria ◽  
Liver And Kidney ◽  
High Concentrations ◽  
Oxidation System

1. Acetylcolletotrichin is a phytotoxic compound that has been isolated from the culture medium of the fungus Colletotrichum capsici (Grove et al., 1966). 2. With isolated liver and kidney mitochondria acetylcolletotrichin markedly inhibited the oxidation of succinate and those substrates with NAD-linked dehydrogenases, but did not inhibit the oxidation of ascorbate in the presence of tetramethyl-p-phenylenediamine. In this respect its action was similar to that of antimycin A. 3. Acetylcolletotrichin differed from antimycin in that, even at high concentrations which produced a maximal inhibitory effect, its action was partially reversed by uncoupling agents. Also acetylcolletotrichin had no detectable effect on the oxidative activity of blowfly flight-muscle mitochondria and was not very effective with heart mitochondria. 4. Acetylcolletotrichin inhibited the oxidative activity of liver mitochondria more markedly when respiration was stimulated by ADP together with phosphate and was less effective when respiration was stimulated by uncoupling agents. 5. There was an unusual interaction between the succinate oxidation system and the oxidation of glutamate together with malate. Thus, glutamate together with malate, even in the presence of rotenone, markedly decreased the effectiveness of acetylcolletotrichin in inhibiting succinate oxidation. 6. These effects were paralleled in the observed redox changes of cytochrome c. 7. The unusual behaviour of the cytochromes b in the presence of acetylcolletotrichin is described, and it is suggested tentatively that this inhibitor acts between cytochromes b with absorption maxima at 30°C of approximately 560 and 565nm.

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