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)

A selective staining of the nucleus of both the cells in an islet (of Langerhans) and the acinar cells could be observed after treatment with bromide-water in an ATPase-medium (calcium-cobalt-method) on a cryostatsection of rat pancreas. Furthermore the behaviour of the other metal ion forming a complex has been tested in place of cobalt salt. As conditioned for the staining reaction the hydrolysis of nucleic acid with oxidation of its base by bromide-water and also the complex formation of Co++ with compounds similar to alloxan, resulted from oxidation were discussed.
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PMID:[The reactive behaviour of the cell nucleus after a pretreatment with a bromide solution and the application of the calcium-cobalt-method for the ATPase evidence (author's transl)]. 7 39

It is known that the negatively stained preparations of inner mitochondrial membrane display characteristic approximately 9 nm F1 (ATPase) knobs projecting from the matrix surface. Freeze-etch studies have reported the absence of such knobs from the "etched" surface of the inner mitochondrial membranes. We have demonstrated their presence on the surface of SMP (submitochondrial particles) prepared by freeze-drying for transmission electron microscopy. This identification has been substantiated by comparison with freeze-dried TU particles (trypsin-urea treated SMP) that are devoid of F1 (ATPase). It has been suggested that a layer of water molecules is strongly adsorbed to the surface of SMP and does not sublime during normal freeze-"etching."
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PMID:Visualization of mitochondrial coupling factor F1(ATPase) by freeze-drying. 9 68

The lipid-free particulate preparations of the mitochondrial ATPase require phospholipid for activity and can be inhibited by oligomycin, as has been demonstrated previously. In this communication a steady state analysis of the activation of a particulate preparation of the ATPase by phospholipids and its subsequent inhibition by oligomycin has been carried out. The relative affinity of the ATPase for purified phospholipids has been determined by measuring the Km for activation (Ka) for several phospholipids. The Ka values varied from 30 to 100 mum. The Vmax in the presence of phosphatides varies from 0.29 to 1.11 mumol ATP hydrolyzed/min/mg of protein; no correlation is noted between the relative affinity of the enzyme for a phospholipid and the V max value. Higher V max values are noted with the more acidic phospholipids, however. Sodium dodecyl sulfate and monoolein also activate with Ka values of 25 and 800 mum, respectively. Diglycerides, however, do not activate. With all lipids the ATPase activity stimulated is oligomycin-sensitive. The Ki values for oligomycin range from 0.1 to 0.6 mum. Oligomycin is a competitive inhibitor with respect to all the phospholipids tested except phosphatidylethanolamine and phosphatidyglycerol. It is also competitive with respect to sodium dodecyl sulfate (k-i equals 0.94 mum). In reciprocal plots of activity versus ATP concentration, with and without oligomycin, an intercept consistent with either mixed or partial noncompetitive inhibition kinetics is noted. Comparable K-i values for oligomycin are obtained when calculated assuming either mixed or partial noncompetitive inhibition. The Km for ATP is the same in the unactivated and the lipid activated particulate ATPase; the value obtained is slightly lower than the Km for ATP in the solubilized, purified ATPase. Using a spectrophotometric assay the time required for activation with phospholipid and inhibition with oligomycin has also been determined. This investigation suggests the possibility that activation of the ATPase is due a position to interact with the water-soluble substrate. Consistent with the above suggestion is the supposition that the lipids do not necessarily confer inhibitor sensitivity to the ATPase, but rather allow an oligomycin-sensitive activity to be expressed.
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PMID:The relationship between the bovine heart mitochondrial adenosine triphosphatase, lipophilic compounds, and oligomycin. 12 47

The effects of deoxycholate, taurocholate and cholate on transport and mucosal ATPase activity have been investigated in the rat jejunum in vivo using closed-loop and perfusion techniques. In the closed-loops, 5 mM deoxycholate selectively inactivated (Na+ + K+)-ATPase, and net secretion of Na+ induced by 2.5 mM deoxycholate was due to reduced lumen to plasma flux of the ion; deoxycholate (2.5 mM) produced marked inhibition of 3-0-methylglucose transport. Luminal disappearance rates of deoxycholate (60.5 plus or minus 2.9% per g wet st of gut) greatly exceeded those of taurocholate (4.3 plus or minus 1.0). In the perfusion studies 1 mM deoxycholate induced net secretion of water, Na+ and C1-, and inhibited active glucose transport; concomitantly "total" ATPase, (Na+ + K+)-ATPase, and Mg-2+-ATPase were inhibited. At higher concentrations (5 mM) deoxycholate stimulated Mg-2+-ATPase activity. Taurocholate and cholate at 1mM had no effect on transport of (Na+ + K+)-ATPase. Mucosal lactase, sucrase and maltase activities were not affected by 1 mM deoxycholate, taurocholate or cholate. These results suggest that deoxycholate inhibits sodium-coupled glucose transport by inhibition of (Na+ + K+)-ATPase at the lateral and basal membranes of the epithelial cell, rather than from an effect at the brush-border membrane level.
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PMID:A comparative study on the effects of different bile salts on mucosal ATPase and transport in the rat jejunum in vivo. 12 87

(1) A water soluble (Ca2+ plus Mg2+)-activated APTase has been extracted with 0.1 mM EDTA and 0.1 mM ATP from human erythrocyte membranes. (2) The specific activity of the extracted protein is increased 4- to 6-fold in comparison with untreated ghosts. (3) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of [gamma-32P]ATP-labeled erythrocyte membranes shows that the (Ca2+ plus Mg2+)-activated ATPase is located in the "spectrin" region (Mr 220 000-240 000). The radioactivity of these high molecular peptide bands is decreased markedly after the extraction of the ATPase at low ionic strength.
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PMID:Extraction and localization of a (Ca2+ and Mg2+)-stimulated ATPase in human erythrocyte spectrin. 12 11

The influence of mixtures of taurocholate (TC), oleic acid (OA), caprylic acid (CA), and monolein (MO) on the toxic effects of deoxycholate (DC) in rat jejunum have been investigated using both a closed loop and perfusion technique. DC induced net secretion of water and electrolytes, inhibited glucose transport and transmural potential difference (PD), and inactivated mucosal "total" and (Na+ -K+)-adenosine triphosphatase. Secretion was reversed to absorption when the instilled or perfused solutions were composed of mixtures of DC, TC and OA; substitution of MO or CA for OA produced a similar effect. DC-induced inhibition of PD, glucose absorption, and mucosal adenosine triphosphatase activity was abolished when DC was mixed with TC and OA. Oleic acid emulsions had no effect on secretion induced by DC. Absorption of DC was inhibited from mixed micellar solutions (TC, OA, DC) but not from pure micellar solutions (TC, DC). These results indicate that the presence of taurocholate and fatty acids or monolein within the intestinal lumen markedly modify a number of the toxic effects of DC on jejunal function. The clinical effects of DC on intestinal function in man may therefore depend on the relative concentrations of other bile salts and lipids within the intestinal lumen.
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PMID:Influence of mixtures of taurocholate, fatty acids, and monolein on the toxic effects of deoxycholate in rat jejunum in vivo. 12 13

Experiments were undertaken to substantiate the hypothesis that the mechanism of the direct effect of ouabain on the renal excretion of electrolytes is the result of inhibition of the transport enzyme, (Na+, K+)-ATPase. In dogs hydrated with saline, an injection of 3H-ouabain into the unilateral renal artery produced a continuing marked increase in excretion of water and sodium from the kidney, but not from the counter kidney. At maximal diuresis -- 90 min after ouabain injection, both kidneys were removed to assay microsomal ATPase activity and determine radioactivity distributed in subcellular structures. It was demonstrated that 3H-ouabain was deposited in the microsome fraction obtained from the injected kidney in concentrations ranging from 10(-7) to 10(-6) M/kg wet weight and (Na+, K+)-ATPase activity of this fraction was inhibited as compared with that of the microsomal fraction obtained from the counter kidney. Since (Na+, K+)-ATPase activity of renal microsomes was significantly inhibited in vitro by more than 10(-7) M of ouabain, ouabain concentration in microsomes obtained from the injected kidney was considered to be sufficient to inhibit ATPase activity. These findings indicate that ouabain diuresis under the present condition is closly related to direct inhibitory effect of ouabain on (Na+, K+)-ATPase activity of microsomes in tubular cells.
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PMID:[Intrarenal distribution and ATPase inhibiting activity of cuabain in dogs (author's transl)]. 12 17

Effects of some chemicals, which are known as inhibitors of Ca2+-dependent ATPases, on the water receptor of the frog tongue were examined by using single fungiform papilla preparations. When a sufficient amount of ruthenium red, quinacrine hydrochloride, ethacrynic acid or 2,4-dinitrophenol was added to the standard stimulating solution (5mM CaCl2+100 mM NaCl), which has been shown to stimulate sufficiently the water receptor of the frog tongue, no neural response was elicited. The concentrations necessary for 50% inhibition were approximately 3 X 10(-6)M for ruthenium red, 1 X 10(-5) M for quinacrine hydrochloride, 1 X 10 (-3) M for ethacrynic acid and 2 X 10(-4) M for 2,4-dinitrophenol. Organic mercurials, mersalyl acid and p-chloromercuribenzoic acid, had no effect on the nueral response, but repeated application of these chemicals led to a permanent depression in receptor activity. Ouabain had no effect on either the neural response or receptor activity. These observations indicate that the receptor molecule of the frog water receptor has a similar property to that of the Ca2+-dependent ATPase of red-cell membrane in respect to the susceptibility to inhibitors.
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PMID:Effects of ruthenium red, quinacrine hydrochloride, ethacrynic acid and 2,4-dinitrophenol on the water receptor of the frog tongue. 12 57

The intracellular sodium, potassium and chloride concentrations in slices of lactating guinea pig mammary gland have been determined by chemical analysis and the use of appropriate values for extracellular space. These ion concentrations after 1 hr incubation at 37 degrees C in a Krebs-Ringer bicarbonate solution are 45mM Na+, 138 mM K+ and 44 mM Cl-, which values are in agreement with those found in fresh mammary gland slices. Inhibition of the NaK activated ATPase cation pump system of the tissue by 10(-4)M ouabain, anoxia or cooling to 0 degrees C Causes a gain of Na+ and an equimolar loss of K+ without a significant change in chloride concentration. The effect of cooling (0 degrees C) is reversible by reincubation at 37 degrees C. Water content of the tissue (76.5% of wet weight) and extracellular space (40.5%) do not change under these conditions. The results permit the conclusion that the NaK activated ATPase system is responsible for the maintenance of the intracellular Na+ and K+ concentrations, but do not support the presence of a chloride pump.
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PMID:Na-KATPase activity and intracellular ion concentrations in the lactating guinea pig mammary gland. Studies on Na-K activated adenosine triphosphatase, XXXVI. 12 7

Fat head minnows, 45-days old, were continuously exposed to DDT using continuous water flow and constant temperature conditions. Exposures were to 0.5 and 2.0 ppb of DDT in water, and combinations of the two concentrations with 50 ppm in food, and 50 ppm in food alone, using C1 4-DDT in food. Brain homogenates were analyzed for enzyme activity from fish treated for 56, 118, 225, and 266 days; and gill analysis was made at 225 and 226 days exposure. Enzyme reductions were greatest in oligomycin-sensitive (mitochondrial) Mg2+ ATPase, with pronounced effects (over 50% inhibition) at the 266th sampling day. In contrast, Na+-K+ ATPase and oligomycin-insensitive Mg2+ ATPase activities were activated by as much as 28% and 40%, respectively. Mitochondrial Mg2+ ATPase of fish brain has been inhibited to the greatest extent in previously reported in vitro studies. All three ATPase enzymes were reduced in gill tissue sampled at the 266th day, with mitochondrial Mg2+ ATPase showing the greatest decline.
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PMID:DDT: effect of continuous exposure on ATPase activity in fish, Pimephales promelas. 12 61


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