Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study was undertaken to localize the enzyme sodium-potassium dependent adenosine triphosphatase in unstimulated human small lymphocytes using the histochemical technique of McClurkin [1964]. The substrate adenosine 5' triphosphate is hydrolyzed by the ATPase resulting in a lead phosphate precipitate at the site of enzyme action, subsequently visualized as lead sulphide. The enzyme was demonstrated in three different patterns, and for each donor the pattern was constant both on all four of the test slides, and on different occasions. The patterns observed were: clusters of granules related to the cell membrane; positive staining localized to portions of the cell membrane, and, less commonly, the whole cell circumference. The significance of this distribution may relate to areas with large numbers of antigen recognition sites on the lymphocyte membrane.
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PMID:Adenosine triphosphatase located on unstimulated human small lymphocyte cell membranes. 14 Apr 12

Bumetanide, a sulfamyl-aminobenzoic acid derivative, is a new and highly effective diuretic agent. The present studies were designed to examine its effects on cation transport in human red cells. At a concentration of 10(-3) M, the drug inhibited both active and passive unidirectional sodium fluxes, as well as active potassium influx. It also caused a significant inhibition of glycolysis. The inhibition caused by bumetanide was less than that seen with ouabain alone, but a bumetanide effect was also present in ouabain-treated cells. Bumetanide had no effect on red cell Na-K adenosine triphosphatase activity and did not affect net transport of sodium in sodium-loaded cells. The data are consistent with a model in which the inhibition of monovalent cation movement in red cells by bumetanide is related to an effect of this compound in decreasing the permeability of the red cell membrane to sodium.
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PMID:The effect of bumetanide on cation transport in human red blood cells. 14 26

1. Serum was collected from normal rats and from rats volume-expanded with isotonic sodium chloride solution. 2. The serum was fractionated by gel filtration on Sephadex G-25 and each fraction was tested for inhibitory activity against sodium-potassium-activated adenosine triphosphatase prepared from rat kidney homogenate. 3. A single low-molecular-weight fraction, eluting after the salts and after exogenously added lysine-vasopressin, had significantly greater enzyme inhibitory activity when obtained from serum of volume-expanded animals than from control serum. 4. As this fraction has been shown in previous independent studies to contain a natriuretic factor, it may be concluded that one property of this factor is the ability to inhibit sodium-potassium-activated adenosine triphosphatase.
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PMID:Circulating inhibitor of sodium-potassium-activated adenosine triphosphatase after expansion of extracellular fluid volume in rats. 14 41

In order to learn whether the kinetics of transient phosphorylation of sodium plus potassium ion transport adenosine triphosphatase was compatible with the hydrolysis of ATP, computer simulation of experimental data was studied. The enzyme mechanism was described in terms of first order and pseudo-first order reactions. The resulting system of linear first order differential equations was solved by a Runge-Kutta method. Phosphorylation kinetics was studied by means of a rapid mixing apparatus at 21 degrees in the presence of 100 micron ATP, 3 mM MgCl2, 120 mM NaCl, and 10 mM KCl. Computer simulation gave a close fit to experimental data with a model of the reaction mechanism which included a sequence of two dephospho forms and two phospho forms of the enzyme. With this model, rate constants obtained by computer simulation were in agreement with constants which had been determined in separate phosphorylation and dephosphorylation experiments. Within experimental limits, the net flux of reaction in each partial step was compatible with the (Na+,K+)-stimulated hydrolysis of ATP (about 324 and 300 nmol-mg-1-min-1, respectively).
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PMID:On the mechanism of sodium- and potassium-activated adenosine triphosphatase. Time course of intermediary steps examined by computer simulation of transient kinetics. 14 33

Coated vesicles from the brain have been purified to near morphological homogeneity by a modification of the method of Pearse. These vesicles resemble sarcoplasmic reticulum fragments isolated from skeletal muscle. They contain proteins with 100,000- and 55,000-dalton mol wt which co-migrate on polyacrylamide gels, in the presence of sodium dodecyl sulfate, with the two major proteins of the sarcoplasmic reticulum fragment. These vesicles contain adenosine triphosphatase (ATPase) activity which is stimulated by calcium ions in the presence of Triton X-100 (Rohm & Haas Co., Philadelphia, Pa.), displaying maximal activity at 8 x 10(-7) M Ca ++. They take up calcium ions from the medium, and this uptake is stimulated by ATP and by potassium oxalate, a calcium-trapping agent. The 100,000-dalton protein of the coated vesicles displays immunological reactivity with an antiserum directed against the 100,000-dalton, calcium-stimulated ATPase of the sarcoplasmic reticulum. As with the sarcoplasmic reticulum fragment, this protein becomes radiolabeled when coated vesicles are briefly incubated with gamma-labeled [32P]ATP. The possible functions of coated vesicles as calcium-sequestering organelles are discussed.
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PMID:Evidence that coated vesicles isolated from brain are calcium-sequestering organelles resembling sarcoplasmic reticulum. 14 39

The adenosine triphosphatase activity of erythrocyte ghosts from patients with Duchenne muscular dystrophy was inhibited by 10(-4) M ouabain to a smaller extent than in normals, when measured in the presence of either high or low concentrations of sodium or potassium ions. The inhibition by ouabain of the enzyme in normal ghosts, measured with low sodium or potassium ions, was less if the erythrocytes were first incubated with plasma from Duchenne patients than if incubated with normal plasma. Similar results were obtained when the ghosts themselves were incubated with Duchenne or normal plasma before assay.
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PMID:Effect of ouabain upon erythrocyte membrane adenosine triphosphatase in Duchenne muscular dystrophy. 14 73

A fine-structural histochemical technique was used to localize magnesium-dependent adenosine triphosphatase (Mg-ATPase) activity in ruminal mucosa. Precipitate appeared on the cytoplasmic surface of the plasmalemma in cells of the upper stratum spinosum, the stratum granulosum, and the deepest layer of the stratum corneum. This ATPase activity was sensitive to glutaraldehyde fixation and possibly to ouabain, but was unaffected by sodium and potassium. The preponderance of Mg-ATPase activity in bovine ruminal epithelium may make it impossible to detect sodium-potassium-activated adenosine triphosphatase ((Na + K)-ATPase) activity histochemically. A Mg-ATPase activity also occurred in mitochondria of the stratum spinosum and stratum granulosum. None of the ruminal sections hydrolyzed adenosine diphosphate, inosine triphosphate, or beta-glycerophosphate when these compounds were used as substitute substrates for adenosine triphosphate. When adenosine-5'-monophosphate was the available substrate, a reaction product appeared in the same layers as Mg-ATPase activity, but the reaction product was confined to the intercellular space.
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PMID:Histochemical localization of adenosine triphosphatase activity in bovine ruminal epithelium. 15 92

The addition of bacteriophage T5 to anaerobic, fermenting cells of Escherichia coli B or K-12 in the presence of 8-anilino-1-naphthalene sulfonate (ANS), N-phenylnaphthyl-1-amine (NPN), or dansyl ethylamine causes the fluorescence of these probes to rise in two steps, the first occurring immediately upon addition, the second delayed by 6 min. The conditions necessary for observing this phenomenon are defined (cell density, probe concentration, substrate, absence of an electron acceptor, multiplicity of infection, growth, and harvesting conditions). The magnitudes of the first and second steps in fluorescence are dependent upon the multiplicity of infection; the timing of the steps is not. The first step correlates with a breakdown in the potassium or rubidium permeability barrier of the cells, and it occurs either aerobically or anaerobically, with fermentable or nonfermentable substrates. The second step occurs only with cells that are without an available electron acceptor, are fermenting, and which have a functional membrane-bound, Ca2+-dependent adenosine triphosphatase (ATPase). The results are consistent with disturbance of energization of the cell membrane by the membrane-bound ATPase at the time of the second step in fluorescence. No changes in the intracellular level of adenosine 5'-triphosphate (ATP) was seen, whereas the extracellular level increased sharply, starting 3--6 min after phage addition. The quantity of ATP found in the medium by 30 min after infection amounted to about four times the amount present inside the cells at the time of infection. The quantity and rate of efflux of ATP was similar under aerobic and anaerobic conditions.
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PMID:Relationship between steps in 8-anilino-1-naphthalene sulfonate (ANS) fluorescence and changes in the energized membrane state and in intracellular and extracellular adenosine 5'-triphosphate (ATP) levels following bacteriophage T5 infection of Escherichia coli. 15 81

The major contractile protein myosin was isolated and characterized from the smooth muscle of human term placentas. Placental myosin originates chiefly in the anchoring villi which bridge the fetal and maternal surfaces of the placenta. The molecular weight of placental myosin is about 460,000; it is composed of two heavy chains of 200,000 molecular weight and two pairs of light chains with 13,500 and 17,500 molecular weights. The adenosine triphosphatase (ATPase) of the myosin is activated by potassium and calcium and it is inhibited by magnesium. Placental actomyosin ATPase is activated by magensium. Contraction and relaxation of the smooth muscle in the anchoring villi are thought to adjust the volume of the intervillous space; thus, actin-myosin interaction is implicated in the regulation of placental hemodynamics.
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PMID:Isolation and characterization of myosin in the human term placenta. 15 81

Hydrogenase and the adenosine 5'-triphosphate (ATP) synthetase complex, two enzymes essential in ATP generation in Methanobacterium thermoautotrophicum, were localized in internal membrane systems as shown by cytochemical techniques. Membrane vesicles from this organism possessed hydrogenase and adenosine triphosphatase (ATPase) activity and synthesized ATP driven by hydrogen oxidation or a potassium gradient. ATP synthesis depended on anaerobic conditions and could be inhibited in membrane vesicles by uncouplers, nigericin, or the ATPase inhibitor N,N'-dicyclohexylcarbodiimide. The presence of an adenosine 5'-diphosphate-ATP translocase was postulated. With fluorescent dyes, a membrane potential and pH gradient were demonstrated.
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PMID:Chemiosmotic coupling in Methanobacterium thermoautotrophicum: hydrogen-dependent adenosine 5'-triphosphate synthesis by subcellular particles. 16 Apr 8


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