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)

In crabs acclimated to low salinity, the activity of Na, K-ATPase from the gills increases; the activity also increases in the antennal glands after acclimation of the animals to high salinity. The activity of Na, K-ATPase in the abdominal ganglion and in the heart does not depend on the salinity to which crabs had been acclimated. Changes in the activity of Mg-ATPase in the gills and antennal glands associated with acclimation of crabs to sea water with different salinity correspond to those in the activity of Na, K-ATPase.
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PMID:[Adenosine triphosphatase activity in the organs of the crab Hemigrapsus sanguineus, acclimated to sea water of different salinity]. 14 82

Red blood cell plasma membranes contain a number of enzymes: ATPases, anion transport protein, glyceraldehyde 3-phosphate dehydrogenase, protein kinases, adenylate cyclase, acetylcholinesterase. Most of them are tightly bound to the membrane and are present in small amounts. As a result, structural characterization of erythrocyte membrane enzymes has not yet been successful. Functional studies have, however, yielded a great deal of information. ATPases allow active transport of cations (calcium, sodium, potassium). Anion transport protein controls movements of chloride and phosphate ions, and of glucose and water. Among glycolytic enzymes: glyceraldehyde 3-phosphate dehydrogenase is partially bound to the membrane. Protein kinases catalyze the phosphorylation of several membrane proteins, one of which (spectrin) is involved in red blood cell mechanical properties. The physiological role of adenylate cyclase is unknown. Acetylcholinesterase is an ectoenzyme. Calcium-dependent ATPase, adenylate cyclase and phosphorylation of erythrocyte membrane proteins have been found abnormal in various conditions: hereditary spherocytosis, sickle-cell anemia, progressive muscular dystrophies, all of these disorders being associated with a decreased deformability of the erythrocyte.
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PMID:The enzymes of the red blood cell plasma membrane. 14 25

The mechanism of plasma membrane turnover was investigated using the duckling salt gland as a model system. Feeding fresh water to salt-stressed ducklings results in a decrease in the Na, K-ATPase in salt gland to non-stressed levels in about 7 days, as measured by ATP hydrolysis and 3H-ouabain binding. Electron micrographs reveal that this is accompanied by a decrease in plasma membrane infoldings on the basal and lateral borders of gland secretory cells. Simultaneously there is an increase in filamentous material and a rise in acid phosphatase and peptidase activities in these cells. Cytochemistry shows that the acid phosphatase activity is mostly associated with the basal or basolateral regions of secretory cells. These ovservations could indicate that the removal of plasma membrane components is accomplished by internalization and digestion within the secretory cells.
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PMID:Ultrastructural, cyto- and biochemical observations during turnover of plasma membrane in duck salt gland. 14 23

An isolation procedure is worked out and properties are studied of CF1 ATPase from chloroplasts with changed submolecular structure. The enzyme, isolated by chlorophorm treatment, produced Ca-dependent ATPase activity in water solution. As compared with the enzyme isolated by well known Lien and Racker method, the enzyme preparation obtained is slightly activated by heating, is not activated by trypsin and has a lesser ability to recover ATP synthesis in EDTA-treated chloroplasts. Purification on DEAE-Sephadex produced the enzyme preparation free of delta-subunit. Chlorophorm treatment is suggested to change submolecular protein structure, in particular, loosening of the link of delta-subunit with other enzyme subunits. The data obtained suggest that delta-subunit participates in the binding of CF1 ATPase with chloroplast membrane.
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PMID:[Isolation and properties of CF1 ATPase chloroplasts with changed submolecular structure]. 14 26

The effect of the adenosine triphosphate analog, 6,6'-dithiobis(inosinyl imidodiphosphate), (sIMP-PNP)2, was tested on the ouabain-sensitive (Na+ + K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) and the ouabain-insensitive Mg2+ - ATPase in microsomes prepared from gill tissue of sea water-adapted rainbow trout, Salmo gairdneri. The (Na+ + K+)-ATPase was completely inhibited by low concentrations of (sIMP-PNP)2 (6 micrometer) but the Mg2+ - ATPase was unaffected by the inhibitor at concentrations as high as 28 micrometer, supporting the suggestion that the two activities represent separate enzymes. The specificity of inactivation could be demonstrated both at a physiological temperature (13 degrees C) and at 37 degrees C. The rates of inactivation were similar at both temperatures. Inactivation of the (Na+ + K+)-ATPase by (sIMP-PNP)2 was reversed by dithiothreitol, suggesting that the inhibitor forms a mixed disulfide with sulfhydryl groups on the enzyme. The inability of substrate (either ATP or its analog, adenyl-5'-yl imidodiphosphate) to protect against inactivation suggests that (sIMP-PNP)2 is reacting with sulfhydryl groups which are not associated with the active site.
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PMID:Inhibition of gill (Na+ + K+)-ATPase in rainbow trout (Salmo gairdneri) by a purinedisulfide analog of adenosine triphosphate. 14 62

The regulation of adrenergic receptors in rat heart was measured in rats made hyperthyroid by injection with thyroxine and made hypothyroid by addition of propylthiouracil to the drinking water. Hyperthyroid rats display cardiac hypertrophy and a decrease in epididymal fat pad weight. The maximal beta-receptor level of ventricular membranes, as determined by (-)-[3H]dihydroalprenolol binding, was increased 60% by thyroxine treatment and decreased about 30% by propylthiouracil treatment. The affinity of the beta receptor was unchanged after thyroxine or propylthiouracil treatment. The maximal activity of the isoproterenol-stimulated adenylate cyclase (EC 4.6.1.1) varied with thyroid state in a manner parallel to the increase in beta-adrenergic binding sites. Thyroxine treatment also increases by 2-fold the beta receptors in isolated rat fat cells. Propylthiouracil treatment lowered the level of alpha receptors in heart by 30% as measured by [3H]dihydroergocryptine binding, but increased the affinity about 2.5-fold. The highest level of alpha receptors was seen in control hearts. These studies indicate that thyroxine may control the turnover of beta-adrenergic receptors in heart and fat cells and regulate physiological responses in these tissues via a hormone-hormone interplay system. Thyroxine treatment reduced the activity of the membrane-bound Mg2+-ATPase (EC 3.6.1.3) and 5'-mononucleotidase (EC 3.1.3.5) but appears to increase the activity of the (Na+ + K+)ATPase (EC 3.6.1.4).
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PMID:Hormone action at the membrane level. VIII. Adrenergic receptors in rat heart and adipocytes and their modulation by thyroxine. 14 63

The hypothesis that colchicine and vinblastine, which are commonly used for therapeutic purposes and known to cause diarrhoea, decrease intestinal water transport by inhibition of Na-K-ATPase activity was tested in rats. Net fluid transport by jejunal segments was measured four hours after intraperitoneal injection of either 0.15 M NaCl (0.5 ml/100 g), colchicine (0.5 mg/100 g b.w.), or vinblastine (1.0 mg/100 g b.w.). Colchicine and vinblastine decreased net fluid transport: 3.0 +/- 0.9 (SE) and 4.6 +/- 0.4 (SE) respectively, as compared to that transported by segments from rats injected with 0.15 M NaCl, 8.6 +/- 0.7 (SE) g fluid/hour/g. Methylprednisolone (3.0 mg/100 g b.w.) abolished the inhibitory effect of cholchicine and vinblastine on fluid transport. Colchicine and vinblastine were found to decrease significantly mucosal Na-K-ATPase activity, 18.2 +/- 4.9 (SE); 25.2 +/- 2.4 (SE) respectively, as compared to that measured in rats injected with saline 40.6 +/- 3.4 (SE) mumol/mg protein/hour. Pretreatment with methylprednisolone prevented the decrease in enzyme activity observed in rats injected with colchicine and vinblastine. The degree of inhibition in intestinal Na-K-ATPase activity was similar to that observed in fluid transport following colchicine and vinblastine. It is thus suggested that colchicine-induced inhibition of water transport is caused by inhibition of Na-K-ATPase activity, an effect which can be prevented by pretreatment with methyl-prednisolone.
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PMID:Effect of colchicine and vinblastine on rat intestinal water transport and Na-K-ATPase activity. 15 Mar 64

The H+-translocating ATPase complex from the thermophilic bacterium PS3 (TF0-F1) is composed of a water-soluble part with ATP-hydrolyzing activity (TF1) and a membrane moiety with H+-conducting activity (TF0). TF0 was obtained by treating TF0-F1 with urea and removing contaminations on a carboxymethyl-cellulose column. This TF0 contained only two kinds of subunits, band 6 protein (13,500 daltons) and band 8 protein (5400 daltons), and it was active in H+ conduction and TF1 binding when reconstituted into proteoliposomes (TF0 vesicles). The binding of TF1 to TF0 present in vesicles restored energy-transducing activities, such as ATP-32Pi exchange, dicyclohexylcarbodiimide-sensitive ATPase, and ATP-dependent enhancement of 8-anilinonaphthalene-1-sulfonate fluorescence. Treatments such as protease digestion and chemical modification with acetic anhydride, succinic anhydride, or diazobenzenesulfonic acid destroyed the TF1-binding activity, which was caused by band 6 protein. Band 8 protein was a proteolipid that reacted specifically with dicylcohexyl-carbodiimide and seemed to play a central role in H+ conduction through the membrane.
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PMID:Resolution of the membrane moiety of the H+-ATPase complex into two kinds of subunits. 15 64

Programmed-feeding polydipsia results in a reliable model of chronic alcoholism in the rat. High oral ethanol comsumption and a predictable withdrawal reaction associated with audiogenic seizures are produced. The maintenance of high blood ethanol levels for three weeks in 18 male Charles River rats was associated with audiogenic seizures after 6 or 8 hours of withdrawal. These chronic alcoholic rats had enhanced blood clearance of ethanol. The cerebral cortical crude mitochondrial fraction showed a decrease in total and magnesium-dependent adenosine triphosphatase activity in alcoholic and control (water-fed) rats compared with normal rats.
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PMID:Programmed feeding as a model of chronic alcoholism in the rat. 15 1

Modification of the carboxyl group with pK 6,8-7,0 of isolated factor F1 by N-cyclohexyl-N'-beta-(4-xethylmorpholine) ethylcarbodiimide (CMCD) leads to the inhibition of the ATPase activity of the enzyme. The reaction rate of factor F1 with CMCD drops in the presence of ATP. It has been shown that during the first stage of the reaction reversible binding of CMCD with factor F1 occurs, forming a stable "enzyme--inhibitor" complex (Kdis=2.10(-4) M). N-cyclohexyl-N'-beta-(4-methylmorpholine) ethylcarbamide, a close analog of CMCD, is a competitive inhibitor of the ATPase reaction with Ki=9.10(-4) M. It is assumed that the carboxyl group, which reacts with CMCD, is located in the catalytic site of factor F1 and serves as the ligand of Me2+ in binding the substrate of the ATPase reaction Me-ATP. The reaction of factor F1, which was modified by CMCD, with proflavine, is accompanied by the covalent binding of the fluorescent label to the enzyme. The binding of proflavine to factor F1 leads to a sharp drop in the solubility of the enzyme in water.
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PMID:[Inhibition of mitochondrial ATPase by water-soluble carbodiimide]. 15 70


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