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Proton-potassium pump

Volume 157. Biomembranes (Part Q ATP-Driven Pumps and Related Transport Calcium, Proton, and Potassium Pumps)... [Pg.22]

Biological membranes show anisotropy, as their molecules are preferentially ordered in a definite direction in the plane of the membrane, and the coupling between chemical reactions (scalar) and diffusion flow (vectorial) can take place. Almost all outer and inner membranes of the cell have the ability to undergo active transport. Sodium and potassium pumps operate in almost all cells, especially nerve cells, while the active transport of calcium takes place in muscle cells. The proton pumps operate in mitochondrial membranes, chloroplasts, and the retina. [Pg.531]

Both the sodium-potassium pump and the proton pump require energy to move particles across the cell membrane. [Pg.111]

Primary active transport systems that have been studied include the sodium-b potassium pump [25,26] (which is the sodium + potassium-activated ATPase) and the calcium ATPase [27] and include also the ATP synthesising proton pumps of mitochondria [18,28]. [Pg.155]

The change from channel to channel is surprisingly easy, and it could have happened both quickly and multiple times. It takes only a handful of changes to turn a particular sodium-potassium channel into a chloride channel. Likewise, a calcium channel can be changed into a sodium channel with a few tweaks, and evidence shows that at least once, when the sodium channel gene was disrupted, a calcium channel substituted and kept this vital function going. For one class of protein pumps, evolution can be traced backward from sodium-potassium pump to copper pump to zinc pump to proton pump. [Pg.226]

Protons are pumped in living systems to establish a proton gradient, and the energy necessary for this pumping is frequently provided by the hydrolysis of ATP, in which ADP and phosphate are formed [7]. In this section, we study a model of a proton pump found in the plasma membrane of plants [8-12] and include the coupling of potassium and calcium ion transport. As in prior examples, we calculate the thermodynamic efficiency [13] of the proton pump with a constant influx of ATP and compare that to the thermodynamic efficiency with an oscillatory influx of ATP, the average of which is the same as the constant concentration of ATP. [Pg.172]

Three kinds of equilibrium potentials are distinguishable. A metal-ion potential exists if a metal and its ions are present in balanced phases, e.g., zinc and zinc ions at the anode of the Daniell element. A redox potential can be found if both phases exchange electrons and the electron exchange is in equilibrium for example, the normal hydrogen half-cell with an electron transfer between hydrogen and protons at the platinum electrode. In the case where a couple of different ions are present, of which only one can cross the phase boundary — a situation which may exist at a semiperme-able membrane — one obtains a so called membrane potential. Well-known examples are the sodium/potassium ion pumps in human cells. [Pg.10]

Vanadate, dioxybis(oxamato)-bond-length ratios, 1,57 Vanadate, heptacyano-potassium salt structure, I, 72 Vanadate, hexafluoro-dipotassium salt history, I, 21 potassium salt history, 1,21 tripotassium salt history, 1,21 Vanadate, pentachloro-stereochemistry, 1,40 Vanadate, pentafluorooxy-stereochemistry, I, 50 Vanadates biochemistry, 3,456 calcium/magnesium ATPase inhibition, 6, 567 competition with phosphates physiology, 6,665 protonation, 3,1026 sodium pump, 6, 557 in uranium purification from ore, 6, 899 Vanadates, hexafluoro-, 3. 482,531 Vanadates, oxoperoxo-, 3,501 Vanadates, pentacarbonyl-, 3, 457 Vanadium biology, 6,665 determination, 1. 548 extraction... [Pg.243]

Omeprazole is classified as a proton pump inhibitor, as it acts by blocking the hydrogen-potassium adenosine triphosphate enzyme system of the gastric parietal cells. Omeprazole therefore inhibits gastric acid release. Common side-effects associated with omeprazole include diarrhoea, headache, nausea and vomiting. Concurrent administration of omeprazole and phenytoin results in enhanced effects of phenytoin, which may lead to phenytoin toxicity. [Pg.119]

This class of enzymes [EC 3.6.1.36] (also known as the hydrogen/potassium-exchanging ATPase, the potassium-transporting ATPase, proton pump, and the gastric H+/K+ ATPase) catalyzes the hydrolysis of ATP to ADP and orthophosphate, coupled with the exchange of and ions. The gastric mucosal enzyme has been the best characterized. [Pg.72]

Mechanism of Action A proton pump inhibitor that selectively Inhibits the parietal cell membrane enzyme system (hydrogen-potassium adenosine triphosphatase) or proton pump. Therapeutic Effect Suppresses gastric acid secretion. Pharmacokinetics ... [Pg.674]

Halorhodopsiti. In addition to bacteriorhodopsin there are three other retinal-containing proteins in membranes of halobacteria. From mutant strains lacking bacteriorhodopsin the second protein, halorhodopsin, has been isolated. It acts as a light-driven chloride ion pump, transporting Cl from outside to inside. Potassium ions follow, and the pump provides a means for these bacteria to accumulate KC1 to balance the high external osmotic pressure of the environment in which they live.578 The amino acid sequences of halorhodopsins from several species are very similar to those of bacteriorhodopsin as is the three-dimensional structure.589 However, the important proton-carrying residues D85 and D96 of bacteriorhodopsin are replaced by threonine and alanine, respectively, in halorhodopsin.590 Halorhodopsin (hR)... [Pg.1335]

The uptake of potassium by microorganisms has been well studied. In the case of E. coli, kinetic investigations on different strains have demonstrated the presence of three or four transport systems. The presence of inducible pathways with widely different Km values for binding K+ allows the cell to accumulate K+ to a constant level under different environments. These transport pathways include those linked to the proton circuit and an example linked to a pump and ATP hydrolysis. Thus the Kdp system is a high affinity pathway with Km = 1 mol dm-3, and involves three proteins in the inner membrane of E. coli, including a K+-stimulated membrane ATPase. The KHA (i.e. K+-H+ antiport) path is driven by proton motive force, while the low affinity system TrKA depends on both ATP and the proton motive force.80,81,82 S. cerevisiae accumulates K+ by K+/H+ exchange.83 Potassium transport may thus be used to control intracellular pH. [Pg.559]

El-Sherif et al. [79] developed and validated a reversed-phase HPLC method for the quantitative determination of omeprazole and two other proton pump inhibitors in the presence of their acid-induced degradation products. The drugs were monitored at 280 nm using Nova-Pak Ci8 column and mobile phase consisting of 0.05 M potassium dihydrogen phosphate-methanol-acetonitrile (5 3 2). Linearity range for omeprazole was 2-36 fig/ml. The recovery of omeprazole was 100.50 0.8%, and the minimum detection was 0.54 /zg/ml. The method was applied to the determination of pure, laboratory prepared mixtures, and pharmaceutical dosage forms. The results were compared with the official USP method for omeprazole. [Pg.221]

Polvani, C. Blostein, R. (1988). Protons as substitutes for sodium and potassium in the sodium pump reaction. J. Biol. Chem. 263,16757-16763. [Pg.120]

Energy is provided, for example, by ATP for pumping sodium ions out of and potassium ions into the cell. Another important example of primary active transport is the proton concentration gradient driven ATP synthesis (Mitchell-hypothesis). [Pg.91]

Hydrogen ions are pumped out of the cell, into the gnt Inmen, in exchange for potassium, through the action of the proton pump potassium is thus effectively recycled (Figure 4.3). [Pg.67]


See other pages where Proton-potassium pump is mentioned: [Pg.84]    [Pg.84]    [Pg.103]    [Pg.809]    [Pg.1032]    [Pg.476]    [Pg.146]    [Pg.149]    [Pg.186]    [Pg.189]    [Pg.492]    [Pg.193]    [Pg.96]    [Pg.180]    [Pg.199]    [Pg.71]    [Pg.1073]    [Pg.156]    [Pg.54]    [Pg.153]    [Pg.40]    [Pg.809]    [Pg.1032]    [Pg.199]    [Pg.173]   
See also in sourсe #XX -- [ Pg.968 ]




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