Calcium/magnesium ATPase

Sandwich complexes nickel. 5, 35 Sapphyrins, 2, 888 demetallation, 2, 891 metallation, 2, 891 reactions, 2, 891 synthesis, 2, 889 Sarcoplasmic reticulum calcium/magnesium ATPase, 6, 566 skeletal muscle... 

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... 

Edelfors S, Raven-Jonsen A. 1992. Effect of organic solvents on nervous cell membrane as measured by changes in the calcium magnesium ATPase activity and fluidity of synaptosomal membrane. Pharmacology and Toxicology 70(3) 181-187. 

Chlorpromazine is a tranquilizer that causes clinical jaundice in 1 % of human users. It decreases sodium-potassium-ATPase and calcium-magnesium-ATPase activity, reducing actin polymerization and membrane fluidity. 

Stefanova, H. I. East, J. M. Gore, M. G. Lee, A. G. Labeling the calcium-magnesium-ATPase of sarcoplasmic reticulum with 4-(bromomethyl)-... 

In binding experiments, the affinity of magnesium ADP to native membranes and to the isolated calcium dependent ATPase was found to be considerably lower than that of magnesium ATP173. On the other hand, from the inhibition of the calcium-dependent ATPase or the activation of calcium release and ATP synthesis apparent affinities for ADP are obtained that are very similar to those of ATP (Fig. 12). The affinity of ADP for the enzyme apparently depends on its functional state. The affinity of ADP for the membranes under conditions of calcium release depends markedly on the pH of the medium. When the medium pH is reduced from 7.0 to 6.0, the affinity drops by a factor of 10. At pH 7.0 the affinity of the membrane for ADP corresponds to the affinity for ATP to the high affinity binding sites in the forward running mode of the pump. In contrast to the complex dependence of the forward reaction on the concentration of ATP, the dependence of the reverse reaction on ADP seems to follow simple Michaelis-Menten kinetics. 

The enzymes called ATP phosphohydrolase are widely distributed in the evolutionary chain and in biological systems. In some cases the ATPase is activated either by magnesium (Mg2+ ATPase) or by calcium (Ca2+ ATPase), and in other cases by both calcium and magnesium (Ca2+ Mg2+ ATPase). Another class of ATPase is stimulated by sodium and potassium and is inhibited by ouabain being denominated Na+ K+ ATPase. There are some ATPases that hydrolyze other nucleotides than ATP, however, with a high preference for ATP. 

Calcium ions (Ca ) are important for the mediation of hepatic injury. Cytosolic free calcium is maintained at relatively low concentrations compared to the extracellular levels. The majority of intracellular calcium is sequestered within the mitochondria and endoplasmic reticulum. Membrane associated calcium and magnesium ATPases are responsible for maintaining the calcium gradient (Farrell et ah, 1990). Significant and persistent increases in the intracellular calcium result from nonspecific increases in permeability of the plasma membrane, mitochondrial membranes, and membranes of the smooth endoplasmic reticulum. Calcium pumps in the mitochondrial membrane require NADPH, thus depletion of available NADPH can cause calcium release from mitochondria (Cullen, 2005). 

ATP is cleaved by most sarcoplasmic reticulum preparations at low rates in the absence of calcium ions. This activity has been denoted as basal activity [20]. When calcium accumulation is initiated, ATP is rapidly hydrolyzed in a calcium-dependent activity, reaching its optimum at a calcium concentration of 10 jaM, and which is severely suppressed by the rising calcium concentrations in the interior of the vesicles [45,64,65]. The calcium-dependent activity was early characterized as the activity of an enzyme distinctly different from the calcium-independent enzyme. In contrast to the calcium-dependent ATPase, the calcium-independent enzyme is quite insensitive to thiol or amino group reagents. Conversely, the calcium-independent activity can be abolished by low concentrations of detergents which do not reduce the activity of the calcium-dependent enzyme [66]. The two enzymatic activities further differ in their nucleotide specificity and affinity, as well as in their magnesium and temperature dependences. The basal activity most likely originates from plasmalemma and T-tubules membranes [41]. 

Calcium plays a vitally important part in possibly as many as three sequences of the contraction—relaxation cycle of vertebrate muscle (Taylor, Lymn and Moll, 1970). In the sarcoplasmic reticulum, calcium is stored in calsequestrin, a protein which holds, with high affinity, 43 atoms of calcium per molecule. The calcium is released in response to nervous impulses and triggers a sequence of reactions that lead to contraction of the muscle. After the contraction, the calcium is pumped back into this reticulum by the calcium/magnesium-dependent ATPase. 

A number of factors have been suspected in calcium transport ionic exchange, a calcium sensitive ATPase, a calcium binding protein, vitamin D, parathormone, cortisone. Calcium uptake is depressed by sodium and enhanced if one-third of the sodium is replaced by mannitol. It appears that sodium is not required for calcium uptake or transepithelial transfer. The intestinal brush border contains a calcium-sensitive magnesium dependent ATPase. In contrast to the K, Na" ATPase, the enzyme is not inhibited by ouabain. Vitamin D induces its appearance. The exact role of the ATPase remains unresolved. 

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