oligomycins and Carcinoma--Ehrlich-Tumor

Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Amino Acids; Amino Acids, Diamino; Animals; Biological Transport, Active; Carcinoma, Ehrlich Tumor; Cell Membrane; Gramicidin; Hydrogen-Ion Concentration; Kinetics; Mice; Models, Biological; Oligomycins; Potassium; Sodium; Time Factors; Valinomycin

Changes in free cytoplasmic Ca2+ ([Ca2+]i) in Ehrlich ascites tumour cells were studied under the effect of deoxyglucose and agents which modify transmembrane Ca2+ fluxes. It was shown that the reason for deoxyglucose-induced [Ca2+]i increase in Ca2+ release from internal stores and the influx from the external medium. Mitochondrial metabolic inhibitors (oligomycin+KCN, oligomycin++uncouplers of oxidative phosphorylation) induce themselves some rise in [Ca2+]i and increase the deoxyglucose effect on [Ca2+]i significantly. The conclusion was made that mitochondria can participate in cytosolic Ca2+ regulation and Ca2+ redistribution in tumour cells.

Topics: Animals; Calcium; Calcium-Transporting ATPases; Carcinoma, Ehrlich Tumor; Cell Membrane; Deoxyglucose; Ion Transport; Oligomycins; Oxidative Phosphorylation; Potassium Cyanide; Terpenes; Thapsigargin; Tumor Cells, Cultured

The effect of the local anesthetic bupivacaine on the energy metabolism of Ehrlich ascites tumor cells has been investigated. Even at low concentrations, bupivacaine decreased the oxygen uptake rate, but its effect was remarkably higher on the uncoupled respiration. Experiments on specific segments of the respiratory chain have shown that bupivacaine did not inhibit electron transport from Q to oxygen. Spectroscopic evidences demonstrated a NAD(P)H oxidation in bupivacaine-treated cells respiring on endogenous substrates, indicating that the inhibition of oxygen depended on a reduced electron transport from site 1-entering substrates to respiratory chain. The aerobic glycolysis was stimulated by low and inhibited by high bupivacaine concentrations. The increased lactate production rate was due to an activation of mitochondrial ATPase, whereas its decrease was related to an inhibition of the hexokinase activity.

Topics: Adenosine Triphosphate; Animals; Bupivacaine; Carcinoma, Ehrlich Tumor; Deoxyglucose; Electron Transport; Energy Metabolism; Glycolysis; Hexokinase; Lactates; Lactic Acid; Male; Mice; Mitochondria; NADP; Neoplasm Proteins; Oligomycins; Ouabain; Oxygen Consumption; Proton-Translocating ATPases; Tumor Cells, Cultured

When Ehrlich ascites carcinoma (EAC) cells and thymocytes were treated with uncoupler or rotenone in glucose-free medium, rapid ATP depletion was observed in both types of the cells. Oligomycin slowed down ATP loss in thymocytes, but not in EAC cells. Thus, mitochondrial ATP hydrolysis appears to be significant in deenergized thymocytes in contrast to EAC cells, in which other ATP consuming reactions were prevailing. Complete deenergization of mitochondria by uncoupler or rotenone in these cells resulted in inactivation of mitochondrial ATPase by 65-75%. The effect was observed after complete and rapid (20-30 s) disruption of the cells with detergent, Lubrol WX. ATPase was blocked by the specific inhibitor protein (IF1) as it was shown by the studies on reactivation of this enzyme. When respiration is blocked but ATP content is supported by glycolysis, mitochondrial ATPase is not suppressed by IF1, and maintains the energization of mitochondria. It is concluded that under complete de-energization of mitochondria IF1 significantly inhibits mitochondrial ATP hydrolysis and may slow down ATP loss in thymocytes and EAC cells.

Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Carcinoma, Ehrlich Tumor; Edetic Acid; Enzyme Activation; Enzyme Reactivators; Hydrogen-Ion Concentration; Hydrolysis; Mitochondria; Oligomycins; Oxidative Phosphorylation; Rats; Rotenone; Thymus Gland

The effect of rhein, 4,5-dihydroxyanthraquinone-2-carboxylic acid, on oxygen consumption and the rate of aerobic and anaerobic lactate production by Ehrlich ascites tumor cells has been investigated. The rate of oxygen uptake decreases with the increase of rhein concentration. Rhein also inhibits aerobic and anaerobic glycolysis. The rate of aerobic lactate production decreases with the drug concentration and the maximal effect was observed at 0.100 mM. Anaerobic lactate production is also inhibited and the maximum effect is reached at 0.220 mM. The possibility that the lactate production decrease was secondary to an effect on mitochondrial ATPase was excluded on the basis of the data with DNP and oligomycin. Rhein reduces the intracellular level of lactate, pyruvate and glucose-6-phosphate. Glucose utilization and 2-deoxy-D-glucose uptake are decreased to the same extent as the inhibition of aerobic lactate production, whereas glucose phosphorylation is unaffected. It is, therefore, concluded that the inhibition of glycolysis of Ehrlich ascites tumor cells by rhein is caused by an impairment of glucose uptake.

Topics: 2,4-Dinitrophenol; Animals; Anthraquinones; Carcinoma, Ehrlich Tumor; Dinitrophenols; Energy Metabolism; Glucose; Glycolysis; Lactates; Lactic Acid; Male; Mice; Oligomycins; Oxygen Consumption; Tumor Cells, Cultured

The effect of Lonidamine, 1-(2,4 dichlorobenzyl)-1-H-indazol-3-carboxylic acid, on the uptake of Adriamycin by Ehrlich ascites tumor cells has been investigated. The uptake of Adriamycin is greatly stimulated by Lonidamine and the increase depends on the energy sources of the cell. In the presence of glucose the intracellular drug content is remarkably lower than that in its absence. This difference lies in the mechanism by which Lonidamine enhances the uptake of Adriamycin. The Adriamycin efflux is via an active transport process and, in the presence of glucose, both aerobic glycolysis and oxidative phosphorylation contribute to ATP synthesis. Although Lonidamine inhibits both these pathways, there is still sufficient ATP to extrude a certain amount of Adriamycin. The elevated intracellular concentration of Adriamycin depends not only on the Lonidamine-inhibited outward transport but also on higher membrane permeability which allows a low concentration of Adriamycin (18 microM) to interfere also with the oxidative metabolism of Ehrlich ascites tumor cells.

Topics: Animals; Biological Transport, Active; Carcinoma, Ehrlich Tumor; Dinitrophenols; Doxorubicin; In Vitro Techniques; Indazoles; Kinetics; Lactates; Male; Mice; Oligomycins; Oxygen Consumption; Pyrazoles

Mouse ascites-tumour cells oxidizing lactate, in a modified Ringer solution, concentrated 2-aminoisobutyrate, L-methionine or 2-(methylamino)isobutyrate about 20-fold from a 0.4 mM solution in the presence of 2-3 micrograms of nigericin/mg cellular dry wt. The ionophore increased cellular [Na+] to almost 100 mM when extracellular [Na+] was about 45 mM. Either valinomycin or the two mitochondrial inhibitors oligomycin and antimycin acting together each markedly lowered the extent to which the tumour cells concentrated amino acid, from the above factor of about 20 to roughly 2-fold. Ouabain (1 mM) had a similar effect, and further raised cellular [Na+]. The sodium pump appeared to be closely involved in amino acid uptake under these conditions.

Topics: Amino Acids; Aminoisobutyric Acids; Animals; Anti-Bacterial Agents; Antimycin A; Carcinoma, Ehrlich Tumor; In Vitro Techniques; Mice; Nigericin; Oligomycins; Ouabain; Potassium; Serum Albumin; Sodium; Valinomycin

The action of lonidamine, 1,(2,4 dichlorobenzyl)-1H-indazol-3-carboxylic acid, on protein synthesis of neoplastic cells growing both in vivo and in vitro has been investigated. Lonidamine decreases amino acid incorporation in all cells tested, although the inhibition is partially relieved by glucose. The inhibition of labeled precursors into acid-insoluble material cannot be ascribed to an impairment of amino acid uptake which, on the contrary, is enhanced by the drug. Tests on cell-free systems showed that lonidamine does not inhibit the tobacco mosaic virus (TMV)-mRNA-directed in vitro protein synthesis, thus indicating that protein synthetic machinery per se is not affected. The inhibition of the rate of protein synthesis achieved by lonidamine must be ascribed to an effect on energy-yielding processes with a mechanism similar to that observed in other metabolic inhibitors. Lonidamine, however, because of its capacity to inhibit both respiration and glycolysis in neoplastic cells, is effective at 10 to 20 times lower concentrations. DNP and oligomycin potentiate the inhibitory effect of lonidamine on the rate of protein synthesis. This finding substantiates the idea that neoplastic cells, including those growing in ascitic form, utilize mitochondrial oxidative phosphorylation as the main source of ATP for their biosynthetic processes.

Topics: Amino Acids; Animals; Antineoplastic Agents; Carcinoma, Ehrlich Tumor; Cell Line; Cell-Free System; Dinitrobenzenes; Glycolysis; Humans; Indazoles; Kinetics; Lactates; Leukemia, Experimental; Male; Melanoma; Mice; Neoplasm Proteins; Oligomycins; Pyrazoles; Rabbits; Sarcoma, Experimental

It has been shown that in the absence of inhibitors of oxidative phosphorylation, changes in fluorescence of 3',3'-diethylthiodicarbocyanine iodide (dis-C2-/5/) in a cell suspension of Ehrlich's ascites carcinoma reflect those in the transmembrane mitochondrial potential. Addition of glucose to the cells in the presence of respiratory inhibitors similar to rotenon induces oscillations in the membrane mitochondrial potential due to H+-ATPase that uses glycolytic ATP. The described changes in energy metabolism parameters are determined by impairment of the interplay between glycolysis and oxidative phosphorylation. The low rate of cytoplasmic NADH oxidation by tumor cell mitochondria favors the latter's accumulation by the cytoplasm and glycolysis inhibition. Pyruvate has been shown to be responsible for NADH oxidation and to remove glycolysis inhibition.

Topics: Animals; Carbocyanines; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; Carcinoma, Ehrlich Tumor; Cells, Cultured; Energy Metabolism; Fluorescent Dyes; Glucose; Kinetics; Luminescent Measurements; Mice; Oligomycins; Oxygen Consumption; Pyrimidine Nucleotides; Quinolines; Rotenone

Topics: Adenine Nucleotides; Animals; Biological Transport, Active; Calcium; Carcinoma, Ehrlich Tumor; Digitonin; Kinetics; Mice; Mitochondria; Oligomycins

The cyanine dye 3,3'-dipropyl-2,2'-thiadicarbocyanine iodide [diS-C3(5)] was found to be a potent inhibitor of endogenous respiration of Ehrlich ascites tumor cells. This effect is believed to involve both rotenone and uncoupler type actions of the dye on the electron transport system of the mitochondria.

Topics: Adenosine Triphosphatases; Animals; Benzothiazoles; Carbocyanines; Carcinoma, Ehrlich Tumor; Dinitrophenols; Electron Transport; Fluorides; Kinetics; Mice; Mitochondria; Oligomycins; Oxygen Consumption; Quinolines; Rotenone

1. The interaction of intact Ehrlich ascites-tumour cells with Ca2+ at 37 degrees C consists of Ca2+ uptake followed by efflux from the cells. Under optimum conditions, two or three cycles of uptake and efflux are observed in the first 15 min after Ca2+ addition. 2. The respiratory substrates malate, succinate and ascorbate plus p-phenylenediamine support Ca2+ uptake. Ca2+ uptake at 37 degrees C is sensitive to the respiratory inhibitors rotenone and antimycin A when appropriate substrates are present. Ca2+ uptake and retention are inhibited by the uncoupler S-13. 3. Increasing extracellular Pi (12 to 30 mM) stimulates uncoupler-sensitive Ca2+ uptake, which reaches a maximum extent of 15 nmol/mg of protein when supported by succinate respiration. Ca2+ efflux is partially inhibited at 30 mM-Pi. 4. Optimum Ca2+ uptake occurs in the presence of succinate and Pi, suggesting that availability of substrate and Pi are rate-limiting. K. Ca2+ uptake occurs at 4 degrees C and is sensitive to uncouplers and oligomycin. Ca2+ efflux at this temperature is minimal. These data are consistent with a model in which passive diffusion of Ca2+ through the plasma membrane is followed by active uptake by the mitochondria. Ca2+ uptake is supported by substrates entering respiration at all three energy-coupling sites. Ca2+ efflux appears to be an active process with a high temperature coefficient.

Topics: Animals; Ascorbic Acid; Biological Transport; Calcium; Carcinoma, Ehrlich Tumor; Energy Metabolism; In Vitro Techniques; Kinetics; Malonates; Mice; Mitochondria; Oligomycins; Phosphates; Succinates; Temperature; Uncoupling Agents

Effects of energy metabolism inhibitors on the granule formation of neutral red in Ehrlich ascite carcinoma cells have no relation with the action of these agents on the ATP formation. Accumulation of neutral red by cells has no relation with granule formation and does not depend on the energy metabolism of cells. The action of 2,4-dinditrophenol, oligomycin, Tween-20, Tween-80 and sodium deoxycholate on the granule formation may be linked with direct action of these agents on the cell membranes, for example, on the Golgi membranes.

Topics: Adenosine Triphosphate; Animals; Antimetabolites; Carcinoma, Ehrlich Tumor; Cytoplasmic Granules; Detergents; Dinitrophenols; Iodoacetates; Mice; Neutral Red; Oligomycins; Oxygen Consumption; Phenazines; Phenylhydrazines

Two membrane fractions prepared from the Ehrlich ascites-tumor cell show non-identical stimulatory responses to certain amino acids in their Mg+2 -dependent activity to cleave ATP, despite the presence of ouabain and the absence of Na+ or K+. The first of these, previously described, shows little (Na+ + K+)-ATPase activity, and is characteristicallly stimulated by the presence of certain diamino acids with low pK2, and at pH values suggesting that the cationic forms of these amino acids are effective. The evidence indicates that these effects are not obtained through occupation of the kinetically discernible receptor site serving characteristically for the uphill transport of these amino acids into the Ehrlich cell. The second membrane preparation was purified with the goal of concentrating the (Na+ +K+)-ATPase activity. It also is stimulated by the model diamino acid, 4-amino-1-methylpiperidine-4-carboxylic acid, and several ordinary amino acids. The diamino acids were most effective at pH values where the neutral zwitterionic forms might be responsible. Among the optically active amino acids tested, the effects of ornithine and leucine were substantially stronger for the L than for the D isomers. The list of stimulatory amino acids again corresponds poorly to any single transport system, although the possibility was not excluded that stimulation might occur for both preparations by occupation of a membrane site which ordinarily is kinetically silent in the transport sequence. The high sensitivity to deoxycholate and to dicyclohexylcarbodiimide of the hydrolytic activity produced by the presence of L-ornithine and 4-amino-1-methyl-piperidine-4-carboxylic acid suggests that the stimulatory effect is not merely a general intensification of the background Mg+ -dependent hydrolytic activity.

Topics: Adenosine Triphosphatases; Amino Acids; Animals; Carcinoma, Ehrlich Tumor; Cell Fractionation; Cell Membrane; Deoxycholic Acid; Enzyme Activation; Hydrogen-Ion Concentration; Kinetics; Magnesium; Mice; Oligomycins; Ouabain; Potassium; Sodium

Ehrlich ascites-tumour cells accumulate Ca2+ when incubated aerobically with succinate, phosphate and rotenone, as revealed by isotopic and atomic-absorption measurements. Ca2+ does not stimulate oxygen consumption by carefully prepared Ehrlich cells, but des so when the cells are placed in a hypo-osmotic medium. Neither glutamate nor malate support Ca2+ uptake in 'intact' Ehrlich cells, nor does the endogenous NAD-linked respiration. Ca2+ uptake is completely dependent on mitochondrial energy-coupling mechansims. It was an unexpected finding that maximal Ca2+ uptake supported by succinate requires rotenone, which blocks oxidation of enogenous NAD-linked substrates. Phosphate functions as co-anion for entry of Ca2+. Ca2+ uptake is also supported by extra-cellular ATP; no other nucleoside 5'-di- or tri-phosphate was active. The accumulation of Ca2+ apparently takes place in the mitochondria, since oligomycin and atractyloside inhibit ATP-supported Ca2+ uptake. Glycolysis does not support Ca2+ uptake. Neither free mitochondria released from disrupted cells nor permeability-damaged cells capable of absorbing Trypan Blue were responsible for any large fraction of the total observed energy-coupled Ca2+ uptake. The observations reported also indicate that electron flow through energy-conserving site 1 promotes Ca2+ release from Ehrlich cells and that extra-cellular ATP increase permeability of the cell membrane, allowing both ATP and Ca2+ to enter the cells more readily.

Topics: Adenosine Triphosphate; Animals; Atractyloside; Biological Transport, Active; Calcium; Carcinoma, Ehrlich Tumor; Cell Fractionation; Cell Line; Magnesium; Mitochondria; Oligomycins; Osmolar Concentration; Oxygen Consumption; Phosphates; Rotenone; Succinates; Trypan Blue

Topics: Aminooxyacetic Acid; Animals; Antimycin A; Aspartate Aminotransferases; Aspartic Acid; Carcinoma, Ehrlich Tumor; Diploidy; Electron Transport; Energy Transfer; Ketoglutaric Acids; Lactates; Mice; Oligomycins; Pyruvates; Rotenone

Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Animals; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; Carcinoma, Ehrlich Tumor; Columbidae; Enzyme Activation; Ethidium; Glutamates; Malates; Mice; Mitochondria, Muscle; Oligomycins; Oxidative Phosphorylation; Oxygen Consumption; Rats; Succinates

This paper describes the uncoupling effect of three isothiocyanates: p-bromophenylisothiocyanate, 4,4'-diisothiocyanatebiphenyl and beta-naphtylemthylisothiocyanate on the respiration of Ehrlich-Lettré cells and isolated mitochondria. The isothiocyanates are similar to other uncouplers (such as 2,4-dinitrophenol and carbonyl cyanide p-trifluoromethoxyphenylhydrazone) in that they: 1. stimulate respiration of state 4 mitochondria; 2. stimulate mitochondrial ATPase activity; 3. release the inhibition of mitochondrial respiration by oligomycin and 4. inhibit both mitochondrial respiration and mitochondrial ATPase activity at higher molar concentrations. The incoupling activity of these isothiocyanates correlates well with their biological activity. Maximal activation of a latent mitochondrial ATPase activity of rat liver mitochondria in the presence of p-bromophenylisothiocyanate was found at a concentration of 15 muM. The investigated isothiocyanates differ significantly in their solubility in organic solvents and their chemical reactivity. We assume that the greater the partition coefficient in a series of isothiocyanates grouped according to the increasing value of log P (partition coefficient for the system octanol/water, 25 degrees C), the greater will be their uncoupling activity, but only up to a certain degree. Any further increase of log P will be marked by a decrease of this activity.

Topics: Adenosine Triphosphatases; Animals; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; Carcinoma, Ehrlich Tumor; Cells, Cultured; Columbidae; Dose-Response Relationship, Drug; Glutamates; Malates; Mitochondria; Mitochondria, Liver; Mitochondria, Muscle; Myocardium; Oligomycins; Oxygen Consumption; Succinates; Thiocyanates; Uncoupling Agents

Topics: Acetates; Animals; Antimycin A; Aspartate Aminotransferases; Aspartic Acid; Benzimidazoles; Carcinoma, Ehrlich Tumor; Electron Transport; Energy Transfer; Hydroxylamines; Kinetics; Lactates; Malates; Mice; Mitochondria; NAD; Nitrogen; Oligomycins; Oxidation-Reduction; Rotenone; Time Factors

Topics: Adenosine Triphosphatases; Amino Acids; Animals; Antimetabolites; Arginine; Carcinoma, Ehrlich Tumor; Cell Membrane; Glycine; Gramicidin; Kinetics; Leucine; Oligomycins; Ornithine; Ouabain; Piperidines; Potassium; Sodium; Valinomycin

Topics: Adenosine Triphosphatases; Animals; Calcium; Carcinoma, Ehrlich Tumor; Dinitrophenols; Enzyme Induction; Glycosides; Magnesium; Mice; Mitochondria; Mitochondria, Liver; Mitochondrial Swelling; Oligomycins; Phenanthrenes; Rats; Stimulation, Chemical

Topics: Animals; Antimetabolites; Antimycin A; Azides; Base Sequence; Carbon Isotopes; Carcinoma, Ehrlich Tumor; Cells, Cultured; Centrifugation, Density Gradient; Cyanides; Dactinomycin; Dinitrophenols; Electrophoresis, Paper; Energy Transfer; Female; Fluorides; Iodoacetates; Kinetics; Mice; Neoplasm Proteins; Neoplasm Transplantation; Neoplasms, Experimental; Oligomycins; Ovarian Neoplasms; Phosphorus Isotopes; RNA; RNA, Neoplasm; Rotenone

Topics: Adenosine Triphosphate; Aminobutyrates; Animals; Biological Transport, Active; Carcinoma, Ehrlich Tumor; Cells, Cultured; Culture Media; Glucose; Oligomycins; Sodium

We have examined the ultrastructure of mitochondria as it relates to energy metabolism in the intact cell. Oxidative phosphorylation was induced in ultrastructurally intact Ehrlich ascites tumor cells by rapidly generating intracellular adenosine diphosphate from endogenous adenosine triphosphate by the addition of 2-deoxyglucose. The occurrence of oxidative phosphorylation was ascertained indirectly by continuous and synchronous monitoring of respiratory rate, fluorescence of pyridine nucleotide, and 90 degrees light-scattering. Oxidative phosphorylation was confirmed by direct enzymatic analysis of intracellular adenine nucleotides and by determination of intracellular inorganic orthophosphate. Microsamples of cells rapidly fixed for electron microscopy revealed that, in addition to oxidative phosphorylation, an orthodox --> condensed ultrastructural transformation occurred in the mitochondria of all cells in less than 6 sec after the generation of adenosine diphosphate by 2-deoxyglucose. A 90 degrees light-scattering increase, which also occurs at this time, showed a t (1/2) of only 25 sec which agreed temporally with a slower orthodox --> maximally condensed mitochondrial transformation. Neither oxidative phosphorylation nor ultrastructural transformation could be initiated in mitochondria in intact cells by the intracellular generation of adenosine diphosphate in the presence of uncouplers of oxidative phosphorylation. Partial and complete inhibition of oxidative phosphorylation by oligomycin resulted in a positive relationship to partial and complete inhibition of 2-deoxyglucose-induced ultrastructural transformation in the mitochondria in these cells. The data presented reveal that an orthodox --> condensed ultrastructural transformation is linked to induced oxidative phosphorylation in mitochondria in the intact ascites tumor cell.

Topics: Adenine Nucleotides; Adenosine Diphosphate; Adenosine Triphosphate; Animals; Carcinoma, Ehrlich Tumor; Cell Line; Hexoses; Histocytochemistry; Kinetics; Male; Mice; Mice, Inbred Strains; Microscopy, Electron; Mitochondria; Nucleotides; Oligomycins; Oxidative Phosphorylation; Oxygen Consumption; Peritoneal Cavity; Phosphates; Pyridines; Scattering, Radiation; Time Factors

Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphate; Animals; Biological Transport, Active; Carcinoma, Ehrlich Tumor; Cell Membrane Permeability; Kinetics; Metabolism; Mice; Nitriles; Oligomycins; Oxidative Phosphorylation; Phenylhydrazines; Phosphates; Phosphorus Isotopes; Phosphotransferases; Rotenone

Topics: Animals; Anti-Bacterial Agents; Antimetabolites; Carcinoma, Ehrlich Tumor; Cytochromes; Cytoplasm; Depression, Chemical; Glucose; Glycolysis; Kinetics; Mice; Microsomes; Mitochondria; Oligomycins; Oxidation-Reduction; Oxidative Phosphorylation; Oxygen Consumption; Polarography; Polyploidy; Pyruvates; Rotenone; Solubility; Spectrophotometry; Stimulation, Chemical; Temperature; Time Factors; Uncoupling Agents; Vitamin K

Topics: Animals; Arsenic; Carcinoma, Ehrlich Tumor; Glucose; In Vitro Techniques; Mitochondria; Oligomycins; Oxidative Phosphorylation; Oxygen Consumption; Phosphates; Uncoupling Agents

Topics: Animals; Anti-Bacterial Agents; Carcinoma, Ehrlich Tumor; Depression, Chemical; Dinitrophenols; Ethacrynic Acid; Glutamates; Kidney; Male; Mitochondria; Mitochondria, Liver; Oligomycins; Oxidative Phosphorylation; Oxygen Consumption; Potassium; Rats; Stimulation, Chemical; Succinates

Topics: Animals; Azides; Biological Transport, Active; Carbon Isotopes; Carcinoma, Ehrlich Tumor; Cell Nucleus; Cold Temperature; Dactinomycin; Fluorides; Glucose; Glycoside Hydrolases; Hemoglobins; Iodoacetates; Mice; Models, Biological; Oligomycins; Oxygen; Puromycin; Rabbits; RNA

Topics: Animals; Biological Transport, Active; Carcinoma, Ehrlich Tumor; Dinitrophenols; Mice; Oligomycins; Ouabain; Oxidative Phosphorylation; Oxygen Consumption; Potassium; Sodium

Topics: Adenosine Triphosphate; Animals; Anti-Bacterial Agents; Biological Transport, Active; Carcinoma, Ehrlich Tumor; Mice; Oligomycins; Ouabain; Oxygen Consumption; Potassium; Sodium

Topics: Adenosine Triphosphate; Animals; Carbon Isotopes; Carcinoma, Ehrlich Tumor; Dinitrophenols; Leucine; Lymphocytes; Male; Neoplasm Proteins; Oligomycins; Oxidative Phosphorylation; Protein Biosynthesis; Rats; Thymus Gland

Topics: Adenine Nucleotides; Adenosine Triphosphate; Animals; Buffers; Carcinoma, Ehrlich Tumor; Culture Techniques; Dicumarol; Dinitrophenols; Fructose; Glucose; Glyceraldehyde; Glycolysis; Hexoses; Manometry; NAD; NADP; Oligomycins; Oxygen Consumption; Phosphates; Pyruvates

Topics: Adenosine Triphosphatases; Animals; Calcium; Carcinoma, Ehrlich Tumor; Dinitrophenols; Fatty Acids; Glycolysis; Magnesium; Mitochondria, Liver; Oligomycins; Ouabain

Topics: Adenosine Triphosphate; Amobarbital; Animals; Antimycin A; Biological Transport, Active; Carcinoma, Ehrlich Tumor; Dinitrophenols; Glucose; In Vitro Techniques; Iodoacetates; Mice; Oligomycins; Potassium; Sodium

Topics: Animals; Anti-Bacterial Agents; Carcinoma, Ehrlich Tumor; Diploidy; Neomycin; Oligomycins