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
1960 ◽  
Vol 199 (4) ◽  
pp. 653-656
Author(s):  
Leonard Share

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.


1991 ◽  
Vol 21 (2-3) ◽  
pp. 151-162 ◽  
Author(s):  
Madhumalti R. Mawal ◽  
Arindam Mukhopadhyay ◽  
Devendra R. Deshmukh

1968 ◽  
Vol 108 (4) ◽  
pp. 619-624 ◽  
Author(s):  
M. M. Bhargava ◽  
A. Sreenivasan

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.


1958 ◽  
Vol 194 (1) ◽  
pp. 47-52 ◽  
Author(s):  
Leonard Share

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.


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

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