Time course of the distribution of in vivo administered89Sr++ in rat liver subcellular fractions

1967 ◽  
Vol 23 (12) ◽  
pp. 1017-1018 ◽  
Author(s):  
E. Carafoli ◽  
R. Tiozzo
Keyword(s):  
Rat Liver ◽  
Time Course ◽  
Subcellular Fractions

scholarly journals The availability of inorganic sulphate in blood for sulphate conjugation of drugs in rat liver in vivo. (35S)Sulphate incorporation into harmol sulphate

1978 ◽  
Vol 172 (2) ◽  
pp. 247-251 ◽  
Author(s):  
G J Mulder ◽  
E Scholtens
Keyword(s):  
Plasma Concentration ◽  
Rat Liver ◽  
Biliary Excretion ◽  
Time Course ◽  
Specific Radioactivity ◽  
Pool Size ◽  
Inorganic Sulphate ◽  
Initial Decrease ◽  
Sulphate Conjugate

1. When Na235SO4 is injected intravenously in rats, it is immediately available for sulphate conjugation of the phenolic drug harmol (7-hydroxyl-1-methyl-9H-pyrido[3,4-b]indole) in the liver. This was established by following the time course of the biliary excretion of the sulphate conjugate of harmol, and the incorporation of [35S]sulphate into harmol sulphate. 2. During the 10min immediately after injection of Na235SO4 re-distribution of [35S]sulphate took place, which resulted in a rapid initial decrease in the plasma concentration of [35S]sulphate; a concomitant decrease in the amount of [35S]sulphate incorporated into harmol sulphate was observed, indicating that the co-substrate of sulphation, adenosine 3′-phosphate 5′-sulphatophosphate, equilibrates rapidly with [35S]sulphate in plasma. 3. The results suggest that the pool size of adenosine 3′-phosphate 5′-sulphatophosphate is very small; therefore the specific radioactivity of [35S]sulphate in plasma determines the specific radioactivity incorporated into sulphate esters at any time.

Stereoselective glutathione conjugation of the separate α-bromoisovalerylurea and α-bromoisovaleric acid enantiomers in the rat in vivo and in rat liver subcellular fractions

1988 ◽  
Vol 37 (1) ◽  
pp. 29-35 ◽  
Author(s):  
Johan M. te Koppele ◽  
Sandra W. Esajas ◽  
Johannes Brussee ◽  
Arne van der Gen ◽  
Gerard J. Mulder
Keyword(s):  
Rat Liver ◽  
Subcellular Fractions ◽  
Glutathione Conjugation

scholarly journals The effect of adrenocorticotrophin on protein degradation in rat adrenal gland and liver

1974 ◽  
Vol 144 (2) ◽  
pp. 397-402 ◽  
Author(s):  
J A Canick ◽  
D B Villee
Keyword(s):  
Adrenal Gland ◽  
Protein Degradation ◽  
Rat Liver ◽  
Exponential Decay ◽  
Total Protein ◽  
Mitochondrial Protein ◽  
Pool Size ◽  
Subcellular Fractions ◽  
The Mean

The rate of adrenal protein degradation appears to be slower in rats to which ACTH (adrenocorticotrophin) has been chronically administered. As measured by the exponential decay of radioactively labelled adrenal protein in vivo, the mean half-lives of total protein and of mitochondrial, microsomal and 18000g-supernatant protein were significantly longer in ACTH-treated animals. Experiments in which either [3H]leucine or NaH14CO3 was used to label proteins showed that of the fractions studied, the effect on mitochondrial protein degradation was most pronounced. The half-lives of the same subcellular fractions in rat liver were not affected by ACTH. The possibility that the results might have been caused by changes in radioisotope reutilization and pool size is discussed.

scholarly journals Effects of ischaemia on content of metabolites in rat liver and kidney in vivo

1970 ◽  
Vol 120 (1) ◽  
pp. 105-111 ◽  
Author(s):  
D. A. Hems ◽  
J. T. Brosnan
Keyword(s):  
Rat Liver ◽  
Glycogen Phosphorylase ◽  
Time Course ◽  
Kidney Cortex ◽  
Redox States ◽  
Renal Ischaemia ◽  
Glycolytic Intermediates ◽  
Liver And Kidney

1. The time-course of changes in content of intermediates of glycolysis in rat liver and kidney cortex after severance of blood supply was investigated. 2. The decline in content of ATP was more rapid in kidney (1.7–0.5μmol/g in 30s) than in liver (2.7–1.6μmol/g in 60s). In both tissues AMP and Pi accumulated. 3. Net formation of lactate was 1.7μmol/g during the second minute of ischaemia in liver from well-fed rats, 1.1μmol/g in liver from 48h-starved rats, and about 1.0μmol/g during the first 30s of ischaemia in kidney. Net formation of α-glycerophosphate was rapid, especially in liver. 4. In kidney the concentration of β-hydroxybutyrate rose, but that of α-oxoglutarate and acetoacetate decreased. 5. In both organs the concentrations of fructose diphosphate and triose phosphates increased during ischaemia and those of other phosphorylated C3 intermediates decreased. 6. The concentration of the hexose 6-phosphates rose rapidly during the first minute of ischaemia in liver, but decreased during renal ischaemia. 7. In kidney the content of glutamine fell after 2min of ischaemia, and that of ammonia and glutamate rose. 8. The redox states of the cytoplasmic and mitochondrial NAD couple in kidney cortex were similar to those in liver. 9. The regulatory role of glycogen phosphorylase, pyruvate kinase and phosphofructokinase is discussed in relation to the observed changes in the concentrations of the glycolytic intermediates.

Subcellular localization of lodinated human kidney α-d-mannosidase in rat liver: Association with subcellular fractions in vivo and in vitro

1980 ◽  
Vol 24 (3) ◽  
pp. 327-335 ◽  
Author(s):  
Dobrivoje E. Marinkovic ◽  
Charles E. Odya ◽  
Jelka N. Marinkovic ◽  
Rajko Igic
Keyword(s):  
Subcellular Localization ◽  
Rat Liver ◽  
Human Kidney ◽  
Subcellular Fractions

scholarly journals The biosynthesis of brain gangliosides. Separation of membranes with different ratios of ganglioside sialylating activity to gangliosides

1977 ◽  
Vol 168 (3) ◽  
pp. 325-332 ◽  
Author(s):  
C A Landa ◽  
H J F Maccioni ◽  
A Arce ◽  
R Caputto
Keyword(s):  
Membrane Fraction ◽  
Time Course ◽  
Mitochondrial Fraction ◽  
Subcellular Fractions ◽  
Synthetase Activity ◽  
Acetylneuraminic Acid ◽  
Mitochondrial Fractions ◽  
Brain Gangliosides

Brain subcellular fractions were analysed for ganglioside-sialylating activity by measuring the incorporation of N-[3H]acetylneuraminic acid from CMP-N-[3H]acetylneuraminic acid into endogenous ganglioside acceptors (endogenous incorporation) and into exogenous lactosyceramide (haematoside synthetase activity). The ratios of endogenous incorporation to gangliosides and of haematoside synthetase to gangliosides for the synaptosomal and mitochondrial fractions from a washed crude mitochondrial fraction were lower than those obtained for other membrane fractions. The differences appear to reflect intrinsic characteristics of each membrane fraction. The results of labelling in vitro and the time course of labelling of gangliosides of the different subcellular fractions in vivo after injection of N-[3H]acetylmannosamine are consistent with the possibility of a subcellular site for synthesis of gangliosides different from that of ganglioside deposition.

scholarly journals In Vivo Effect of Uncoupling Agents on the Incorporation of Calcium and Strontium into Mitochondria and Other Subcellular Fractions of Rat Liver

1967 ◽  
Vol 50 (7) ◽  
pp. 1849-1864 ◽  
Author(s):  
E. Carafoli
Keyword(s):  
Oxidative Phosphorylation ◽  
Rat Liver ◽  
Liver Cell ◽  
Intact Animal ◽  
Specific Activity ◽  
Mitochondrial Fraction ◽  
Liver Cells ◽  
Subcellular Fractions ◽  
Mitochondrial Oxidative Phosphorylation

After injection of 45Ca++ or 89Sr++ into rats, the largest part of the radioactivity in the liver cell is associated with the subcellular structures, only negligible amounts of it being found in the soluble hyaloplasm. 50 % or more of the 45Ca++ and 89Sr++ in the liver cell is recovered in the mitochondrial fraction. The specific activity of Ca++ after injection of 45Ca++ is far greater in mitochondria than in microsomes. Pretreatment of the rats with uncouplers of oxidative phosphorylation markedly decreases the amount of radioactivity associated with the mitochondrial fraction. The amount of radioactivity recovered in the microsomes and in the final supernatant on the contrary increases. These effects are present only when mitochondrial oxidative phosphorylation is completely uncoupled. The Ca++ content of mitochondria from the livers of rats pretreated with uncouplers is sharply decreased with respect to the controls. It is concluded that in the liver cells of the intact animal energy-linked movements of Ca++ and Sr++ take place in mitochondria.

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