Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two nitroxyl spin label (NSL) compounds that are used experimentally as in vivo contrast enhancers in magnetic resonance (MR) imaging were tested for acute toxicity in rats and for genotoxic effects in cell cultures. These compounds, 2,2,5,5-tetramethyl-1-pyrrolidinyl-oxy-3-carboxylic acid (PCA) and 2,2,6,6-tetramethyl-1-oxido-4-piperidinyl-1-succinic acid (TES) and their hydroxylamine and amine derivatives did not induce sister chromatid exchanges or mutations in Chinese hamster ovary cells at the HGPRT or Na+/K+ ATPase loci. The acute LD50 doses in rats for PCA and TES are 15.1 mmol/kg or greater, suggesting relatively high tolerance.
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PMID:Nitroxyl spin label contrast enhancers for magnetic resonance imaging. Studies of acute toxicity and mutagenesis. 651 Dec 62

Procyclic culture forms of Trypanosoma brucei stock 427 have been screened for the presence of enzymes involved in glycolysis, mitochondrial energy metabolism and threonine degradation. The enzyme activities in the procyclics were compared with those of the blood stream forms. The specific activities of glycolytic enzymes represented 30-70% of the respective levels in the blood stream form, except for hexokinase which was 25-fold reduced. Cell fractionation showed that the enzymes involved in the early sequence of the glycolytic pathway, i.e. from hexokinase to phosphoglycerate kinase, and the enzymes NAD+-linked glycerol-3-phosphate dehydrogenase and glycerol kinase were all present in glycosomes equilibrating at a density of 1.23 g/cm3 in sucrose gradients. Malate dehydrogenase was 8-fold more active in procyclics than in bloodstream forms. This increase in activity was the result of the appearance of malate dehydrogenase in the glycosomes of the procyclics, in addition to mitochondrial and cell-sap activities which were present in both stages of the life cycle. Glycosomes contained part of the adenylate kinase activity, which was also associated with the mitochondrion. Succinate dehydrogenase and sn-glycerol-3-phosphate dehydrogenase, together with oligomycin-sensitive ATPase, were located in the mitochondrion which had a density in sucrose ranging from 1.16 to 1.18 g/cm3. This organelle also contained L-threonine 3-dehydrogenase and carnitine acetyltransferase, two enzymes involved in threonine catabolism. The latter two enzymes had activities which were, respectively, 15-and 13-fold higher in the procyclics than in the bloodstream form. Mitochondrial sn-glycerol-3-phosphate dehydrogenase was decreased 4-fold.
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PMID:Localization of malate dehydrogenase, adenylate kinase and glycolytic enzymes in glycosomes and the threonine pathway in the mitochondrion of cultured procyclic trypomastigotes of Trypanosoma brucei. 680 9

The temperature dependence of various activities related to the energy metabolism of isolated membranes and whole cells of the thermophilic bacterium Chloroflexus aurantiacus was determined after phototrophic growth at either 40, 50, or 60 degrees C. The data obtained were expressed by use of Arrhenius plots. Maximum activities were determined at about 65 degrees C for succinate 2,4-dichlorophenol-indophenol reductase as well as NADH oxidase and at about 70 degrees C for Mg-ATPase and for light-induced proton extrusion by cells. Activation energies for Mg-ATPase and light-induced proton extrusion were about 40 kJ mol-1 from 30 degrees C to about 50 degrees C and they increased significantly at higher temperatures. Essentially the same dependency was detectable with NADH oxidase, except for an increase in activation energy below 41 degrees C. All of these responses were independent of growth temperature. Succinate-2,4-dichlorophenol-indophenol reductase showed a change in activation energy around 41 degrees C only with cells grown at 60 degrees C. Differences in the responses of cells grown at different temperatures were identified on the basis of changes from sigmoidal to hyperbolic kinetics for light saturation of proton extrusion. Moreover, the thermostability of proton extrusion was maximal when assayed at the corresponding growth temperatures. In any case, thermostability was lowest at the 65 and 68 degrees C assay temperatures. Differential scanning calorimetry with membranes revealed irreversible heat uptake from about 60 to 72 degrees C. The results are discussed in light of the activation energy for the specific growth rate, which is lowest at temperatures from 40 degrees C to the optimum at 60 degrees C.
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PMID:Temperature dependence of growth and membrane-bound activities of Chloroflexus aurantiacus energy metabolism. 686 22

At 20 degrees when active transport of an organic acid - fluorescein in superficial proximal tubules of surviving rat kidney does not depend on the external Na, the capability of acetate (as well as succinate and D,L-leucine) of stimulating the fluorescein uptake in the tubules was studied. As it turned out, acetate and leucine stimulated the fluorescein uptake at 120 mM of Na in the bath medium but had no effect at 10 mM of Na. Succinate has a biphasic effect on the fluorescein transport (stimulation at low succinate concentration), which does not depend on Na concentration in the medium. The effect of acetate disappears with the presence of ouabain in the medium. The stimulation of fluorescein uptake by acetate is accompanied by somewhat increased degree of reduction of cellular pyridine nucleotides. Pyridine nucleotides are reduced more markedly in the presence of ouabain or in the absence of Na from the bath medium. The disappearance of acetate effect on the fluorescein transport is explained by the fact of transition of cell mitochondria in the inactive state 4, due to the decrease in the level of cellular ADP when Na, K-ATPase is inhibited by ouabain or by diminution of tissue Na+ concentration.
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PMID:[Effect of acetate on Na+-independent organic acid transport in the proximal tubules of the rat kidney]. 709 46

Anaerobic threshold (AT) and maximum oxygen uptake (max VO2) were determined in 15 young female cross-country skiers, aged 15--20 years, during incremental bycycle ergometer exercise. Succinate dehydrogenase (SDH), malate dehydrogenase (MDH), citrate synthase (CS) and lactate dehydrogenase (LDH) were analyzed biochemically and percentage of slow twitch fibres (%ST fibres, myosin adenosine triphosphatase staining) histochemically in muscle samples obtained from m. vastus lateralis. Max VO2 correlated significantly with anaerobic threshold in ml x kg-1 x min-1 (mlAT) but when AT was expressed in percent of max VO2 (%AT) the correlation was insignificant. Significant correlations were found between %AT and SDH (r = 0.63) and between mlAT and CS (r = 0.58). Max VO2 showed no significant correlations with the enzymes studied or %ST fibres. The results of the study seem to support the hypothesis that anaerobic threshold is related to oxidative capacity of muscle.
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PMID:Anaerobic threshold, skeletal muscle enzymes and fiber composition in young female cross-country skiers. 737 21

We developed an improved determination method of mitochondrial proton adenosine triphosphatase (ATPase) activity in the liver. The activity was measured fluorometrically with a 3,3'-dipropylthiodicarbocyanine iodide (diS-C3(5)), which is excited at 625 nm and emits fluorescence at 670 nm. This dye transmits the electric potential across the inner mitochondrial membrane. The fluorescence intensity of diS-C3(5) with mitochondria (100 microliters, 4-16 mg/ml protein) in a 2 ml potassium buffer (pH 7.4) was regarded as a standard electric potential. After confirming the activity of the mitochondrial electron transport chain by succinic acid (9 mumol), we inhibited the chain by antimycin A (1.25 micrograms). Fluorescence intensity decreased by adenosine 5'-triphosphate (ATP) (2 mumol) and oligomycin (25 micrograms) inhibited this depression. The value of mitochondrial proton ATPase activity was calculated as a percentage of the fluorescence intensity change by ATP per the standard electric potential. The activity of mitochondrial proton ATPase in the normal fresh rat livers was 50.3 +/- 2.2%. Good correlation (r2 = 0.807) between two methods for mitochondrial proton ATPase activity, our newly developed method and a conventional colorimetric method, was obtained in the rat livers with various conditions. This method has advantages that the proton ATPase activity can be measured in intact mitochondria, and all procedures can be completed within 40 min. It is suitable for the determination of mitochondrial viability of liver graft in the hepatic resections and transplantations.
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PMID:Rapid fluorometric assay for mitochondrial proton adenosine triphosphatase activity for assessment of viability of liver graft tissue. 786 82

Transgenic mice can be created to serve as models of human cardiac disease. Despite the technology available to manipulate the cardiovascular system of the mouse, there is relatively little information available concerning the normal physiology of the mouse heart. Therefore, we have characterized the response of the adult mouse to chronic physical conditioning by swimming. Adult female C57/B16 mice were conditioned by swimming up to 90 min twice daily for 4 wk, resulting in a 10% increase in heart weight and a 16% increase in heart weight-to-body weight ratios compared with sedentary controls. The heart rate response to a submaximal work load decreased > 20% with this conditioning program. Succinate dehydrogenase activity increased markedly in the soleus muscles of the conditioned animals, from 28 +/- 3 to 44 +/- 3 nmol.mg-1.min-1. In contrast to these changes, which also characterize the exercise model in the rat, no increase in cardiac tissue norepinephrine content or in cardiac myosin or myofibrillar adenosinetriphosphatase (ATPase) activities was observed, and no change in the V1 predominant myosin isoform or alpha-myosin heavy chain mRNA profiles was seen in the hearts of the swimmers. This study establishes that mice are able to develop cardiac hypertrophy in response to chronic conditioning which is not associated with changes in the ATPase activities of cardiac muscle. These data should be of use to investigators using murine models to define the molecular basis of adaptive cardiac hypertrophy in vivo.
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PMID:Cardiac adaptations to chronic exercise in mice. 809 82

Effect of the polycation on oxidative phosphorylation in the rat liver mitochondria has been studied. Both oxygen uptake and coupled phosphorylation were progressively inhibited by increasing concentration of the polycation, as observed with NAD-linked substrates, succinate and ascorbate+TMPD which activates the terminal part of the respiratory chain. NADH oxidase, NADH dehydrogenase and cytochrome oxidase were strongly inhibited by the polycation, 80-90% of the activity being lost at an inhibitor concentration of 100 microM. Succinate oxidase and succinate dehydrogenase were inhibited 60-66% at 100 microM concentration of the polycation. The polycation inhibited the uncoupler 2,4-dinitrophenol stimulated ATPase activity both in presence and absence of Mg2+ ions. The polycation also inhibited salt-induced volume change.
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PMID:Inhibition of mitochondrial oxidative phosphorylation and its electron transport pathway by a polycation in vitro. 850 25

In the rat diaphragm muscle, the histochemical classification of type I, IIa, IIb, or IIx fibers was correlated with myosin heavy chain (MHC) immunoreactivity. Expression of MHC isoforms in single dissected fibers was also assessed electrophoretically. Most fibers (approximately 86%) expressed a single MHC isoform, and when present, coexpression of MHC-2X and MHC-2B isoforms was most prevalent. Type I and IIa fibers were the smallest, type IIb fibers were the largest, and type IIx fibers were intermediate. Succinate dehydrogenase (SDH) and calcium-activated myosin adenosinetriphosphatase (actomyosin ATPase) activities were measured with quantitative histochemical procedures. Type I and IIa fibers had the highest SDH activities, followed in rank order by type IIx and IIb fibers. Type I fibers had the lowest actomyosin ATPase activity, followed in rank order by type IIa, IIx, and IIb fibers. Across all fibers, there was an inverse relationship between fiber SDH activity and cross-sectional area and a positive correlation between fiber actomyosin ATPase activity and cross-sectional area. The SDH and actomyosin ATPase activities of muscle fibers were also inversely correlated. These phenotypic differences in SDH and ATPase activities may be important in determining the contractile and fatigue properties of different fiber types in the rat diaphragm muscle.
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PMID:SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle. 859 23

The rapid in vivo activation of Saccharomyces cerevisiae plasma membrane H+-ATPase that has been attributed to medium acidification from pH 6.5 to pH 3.5 is not caused by the low pH itself but is induced by the weak organic acid (succinic) used as the acidulant. The activation induced by 50 mM succinic acid at pH 3.5 occurred in both the presence or absence of glucose. Activation at pH 3.5 was also induced by acetic acid and it was maximal at 50 mM concentration. To investigate the role of plasma membrane ATPase activation in pH homeostasis, the internal pH (cytosolic and vacuolar) of yeast cells incubated in media at pH 6.5 or at pH 3.5, acidified either with HCl or acetic acid, were compared by using in vivo (31)P-NMR. Despite plasma membrane ATPase activation by acetic acid, the decrease in cytosolic pH caused by external acidification was much more important when the permeant acetic acid was used instead of HCl as the acidulant. The supplementation of the incubation medium at pH 3.5 with glucose led to higher cytosolic pH values, consistent with the observed in vivo activation of plasma membrane ATPase by glucose. At the external pH value of 6.5 the vacuole was maintained at a mildly acidic pH (around 6) while the cytosol was at about neutral pH; however, when cytoplasmic pH decreased due to external acidification, vacuolar pH accompanied that decrease. Vacuolar pH reached 5.4-5.5 during incubation with HCI and dropped sharply to values below 4.4 in cells incubated with acetic acid. These results indicate that the vacuole also plays a role in homeostasis of the intracellular pH.
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PMID:Effect of extracellular acidification on the activity of plasma membrane ATPase and on the cytosolic and vacuolar pH of Saccharomyces cerevisiae. 910 83


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