Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

The purification of axonal membranes of crustaceans was followed by measuring enrichment in [3H]tetrodotoxin binding capacity and in Na+, K+-ATPase activity. A characteristic of these membranes is their high content of lipids and their low content of protein as compared to other types of plasmatic membranes. The axonal membrane contains myosin-like, actin-like, tropomyosin-like, and tubulin-like proteins. It also contains Na+, K+-ATPase and acetylcholinesterase. The molecular weights of these two enzymes after solubilization are 280,000 and 270,000, respectively. The molecular weights of the catalytic subunits are 96,000 for ATPase and 71,000 for acetylcholinesterase. We confirmed the presence of a nicotine binding component in the axonal membrane of the lobster but we have been unable to find [3H]nicotine binding to crab axonal membranes. The binding to axonal membranes og of the sodium channel, has been studied in detail. The dissociation constant for the binding of [3H]tetrodotoxin to the axonal membrane receptor is 2.9 nM at pH 7.4. The concentration of the tetrodotoxin receptor in crustacean membranes is about 10 pmol/mg of membrane protein, 7 times less than the acetylcholinesterase, 30 times less than the Na+, K+-ATPase, and 30 times less than the nicotine binding component in the lobster membrane. A reasonable estimate indicates that approximately only one peptide chain in 1000 constitutes the tetrodotoxin binding part of the sodium channel in the axonal membrane. Veratridine, which acts selectively on the resting sodium permeability, binds to the phospholipid part of the axonal membrane. [3H]Veratridine binding to membranes parallels the electrophysiological effect. Veratridine and tetrodotoxin have different receptor sites. Although tetrodotoxin can repolarize the excitable membrane of a giant axon depolarized by veratridine, veratridine does not affect the binding of [3H]tetrodotoxin to purified axonal membranes. Similarly, tetrodotoxin does not affect the binding of [3H]veratridine to axonal membranes. Scorpion neurotoxin I, a presynaptic toxin which affects both the Na+ and the K+ channels, does not interfere with the binding of [3H]tetrodotoxin or [3H]veratridine to axonal membranes. Tetrodotoxin, veratridine, and scorpion neurotoxin I, which have in common the perturbation of the normal functioning of the sodium channel, act upon three different types of receptor sites.
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PMID:Constitution and properties of axonal membranes of crustacean nerves. 0 58

Adenosine 5'-triphosphate (ATP) synthesis driven by an artificially imposed membrane potential in right-side-out membrane vesicles of Escherichia coli was investigated. Membrane vesicles prepared in the presence of adenosine diphosphate were loaded with K+ by incubation with 0.5 M potassium phosphate. Addition of valinomycin resulted in the synthesis of 0.2 to 0.3 nmol of ATP/mg of membrane protein, whereas no synthesis was observed after addition of nigericin. Addition of K+, dicyclohexylcarbodiimide, carbonylcyanide p-trifluoromethoxyphenylhydrazone, or azide to the assay buffer inhibited ATP synthesis. Adenosine diphosphate and Mg2+ were found to be required. Ca2+, which can replace Mg2+ for the hydrolytic activity of the Mg2+-adenosine triphosphatase (ATPase) (EC 3.6.1.3), could not replace Mg2+ in the synthetic reaction and, in fact, inhibited ATP synthesis even in the presence of Mg2+. Strain NR-70, a mutant lacking the Mg2+-ATPase, was unable to synthesize ATP using an artificially imposed membrane potential. Additionally, the Mg2+-ATPase was found to contain tightly bound ATP.
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PMID:Adenosine 5'-triphosphate synthesis energized by an artificially imposed membrane potential in membrane vesicles of Escherichia coli. 0 30

Membrane vesicles from Azotobacter vinelandii O prepared by osmotic lysis of spheroplasts in tris (hydroxymethyl) aminomethane/acetate buffer (pH 7.8) contain a latent adenosine triphosphatase (ATPase). The ATPase can be activated when the vesicles are incubated in the presence of an electron donor (D-lactate) and a mixture of adenosine diphosphate and inorganic phosphate or by controlled treatment with trypsin. After the ATPase is activated, the membrane vesicles in the presence of adenosine triphosphate accumulate calcium but not glucose or rubidium (in the presence of valinomycin). ATP-dependent calcium uptake follows Michaelis-Menten kinetics with a Km of 48 muM and a Vmax of 20 nmol/min/mg of membrane protein and is highly specific for calcium over cations magnesium, barium, lanthanum, sodium, potassium, and lithium. The calcium accumulated in the presence of ATP is freely exchangeable with external calcium and is rapidly released in the presenceof uncouplers or ATPase inhibitors. Calcium uptake in the presenceof ATP is blocked by dicyclohexylcarbodiimide, ADP, p-chloromercuriphenylsulfonate, by the proton-conducting ionophores m-chlorophenylcarbonylcyanide hydrazone, nigericin, monensin, and gramicidin D, but not by potassium cyanide, anoxia, or valinomycin (in the presence of potassium). Measurements of the external pH of vesicle suspensions reveal that protons are actively taken up by the membranes during hydrolysis of ATP. These results suggest that vesicles prepared under these conditions have a topology which is inverted with respect to the intact cell and that calcium is accumulated by means of proton antiport.
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PMID:ATP-dependent calcium transport in isolated membrane vesicles from Azotobacter vinelandii. 0 92

A membrane fraction enriched in parathyroid hormone (PTH)-sensitive adenylate cyclase and sodium and potassium ion-activated (Na+, K+)-ATPase was prepared from bovine kidney. Tritiated PTH binding to this membrane fraction was dependent on both hormone and membrane protein concentration. Both total and specific binding of the hormone decreased significantly after 5 to 10 min of incubation at 22 degrees. PTH binding was highly specific, being sensitive to inhibition only with active forms of unlabeled hormone (native and 1-34 PTH). Specific binding showed a pH optimum of 7.3 to 7.5. Inhibition of binding of tritiated hormone by unlabeled PTH was also highly effective at pH 6.0, but this apparently specific binding was also inhibited by adrenocorticotropic hormone, insulin, glucagon, and vasopressin. Dissociation of bound hormone was demonstrated, and an apparent dissociation constant of 4.6 X 10(-2) min-1 was obtained. Specific binding was eliminated by pretreatment of the membranes with trypsin. The concentration dependence for inhibition of binding with unlabeled PTH was identical to that for activation of adenylate cyclase in this membrane preparation, and binding was also inhibited by concentrations of calcium in the 0.5 to 2 mM range.
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PMID:Binding of tritiated bovine parathyroid hormone to plasma membranes from bovine kidney cortex. 1 29

The reactions of adenosine 14C-and gamma 32P-labelled ATP with isolated membranes from catecholamine storage vesicles of the bovine adrenal medulla were studied. In presence of Mg2+ about twice as much of 32P-radioactivity combined with the membrane as 14C-adenosine compounds at 31 degrees C and also at 0 degrees C, while in the absence of Mg2+ the amounts of 14C and 32P incorporated were similar for both substances. Autoradiography of the SDS-polyacrylamide gel after electrophoresis of the 32P-ATP-treated membrane protein showed two distinct zones corresponding to protein bands. Sonication released twice as much 32P-ATP as 14C-ATP from the space within the membrane particles indicating that at least half of the ATP present in space did not contain its original terminal phosphate group. About 40--45% of the 32P-radioactivity was incorporated in the membrane lipids, whereas only small amounts of 14C-radioactivity were extracted with lipids. About 1/3 of the incorporated 14C-radioactivity was not extractable with acids. The same amount remained in the 32P-ATP treated preparation acid-stably bound after extraction of the lipids and hus must be firmly bound ATP. When the reaction of the membrane preparation with labelled ATP was performed at 0 degrees C the fractions of the acid-stably bound 32P- and 14C-radioactivity increased. About 1 nmole/mg of protein (10--15%) of the bound 32P-radioactivity was exchangeable against unlabelled ATP, while only a very small fraction (less than 0.5 nmol/mg protein) of the 14C-radioactivity was exchanged against unlabelled ATP. Preincubation of the membrane particles with ATP-Mg2+ at 0 degrees C induced 30% inhibition of the ATPase activity and abolition of the net uptake of catecholamines. Different Km values obtained from initial velocity studies of ATPase activity and the overall-incorporation of 32P-radioactivity indicated that a direct correlation between these processes did not exist. Different strong inhibitory effects exerted by ADP on the ATPase activity and net uptake of catecholamine at the one hand and the overall 32P-and 14C-incorporation at the other hand supported that view. It is concluded that small fractions of the observed 32P-and 14C-incorporation can be involved in the ATP hydrolyzing reaction.
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PMID:Distribution and metabolic fate of adenosine nucleotides in the membrane of storage vesicles from bovine adrenal medulla. 4 49

There is evidence that membrane proteins can serve as the functional units of ionic transport in biological membranes. Laser Raman spectroscopy has been used to probe specific molecular interactions inside two models of transport membrane proteins, valinomycin and gramicidin A. Conformational changes of these molecules, as well as specific interactions with ions, can be detected and may help elucidate how membrane transport proteins such as Na+ minus K+ ATPase and rhodopsin function. Resonance Raman spectroscopy has also been used to study conformational changes and protein-chromophore interactions in rhodopsin, the membrane protein that acts as the primary unit of visual excitation in the eye.
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PMID:Models of ionic transport in biological membranes. Raman spectroscopy as a probe of valinomycin, gramicidin A', and rhodopsin conformations. 4 37

The non-ionic detergent octyl glucoside solubilizes a substantial amount of Streptococcus faecalis membrane protein without loss of the monitored enzyme activities. A secondary detergent, dioctanoyl phophatidycholine, appears to increase the yield of solubilized material. In addition, the effect of ionic strength indicates that it may be possible to selectively extract groups of membrane proteins by their characteristic solubility at different ionic strengths. The solubilized membrane-associated enzymes, ATPase and NADH dehydrogenase, enter polyacrylamide gels as distict species. Electrophoretic studies suggest that there are two membrane-associated ATPase in the Streptococcus faecalis, one which dissociates from the membrane in the absence of Mg-2+ ions and the other which remains particulate until solubilized by detergents. Octyl glucoside can be easily removed from a solution containing solubilized proteins and lipid by dialysis.
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PMID:Solubilization of bacterial membrane proteins using alkyl glucosides and dioctanoyl phosphatidylcholine. 12 71

In the present paper the mechanism of the adenosine formation by a mixture of nerve ending and transmitter granula fractions was invesitgated. The adenosine formation in vivo is only possible via the whole degradation chain ATP - ADP - AMP - adenosine. The enzymes involved are ATPases, adenylate kinase and 5'-nucleotidase. The ATPase and adenylate kinase effectors Ca++ and Mg++ can be regarded as trigger ions switching on and off the degradation chain. The adenylate kinase represents a key enzyme within the whole chain. In the ion-activated state a non-inhibited adenosine formation was observed, when the initial ATP concentration amounted to less than 0,1 muMol per mg synaptosomal membrane protein. Under these conditions the whole chain velocity is mainly dependent on the 5'-nucleotidase concentration, because ATPases and adenylate kinase remove the nucleotidase inhibitors ATP and ADP spontanously. The conditions for the optimal velocity of the adenosine formation at the synaptic membrane in vivo in all probability are present. A hypothesis for the mechanism of the synaptic adenosine formation in vivo was developed. The importance of this process in respect to the synaptic transmission was discussed.
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PMID:[Mechanism of synaptosomal degradation of ATP in connection with involvement of adenosine in the transmission process]. 12 26

(Na+ + K+)-activated ATPase in beef brain microsomes is inactivated by the disulfide of thionosine tri[gamma-32P]phosphate, an ATP analog. The inactivation of the enzyme, which is accompanied by an incorporation of radioactivity into the membrane protein, is abolished by ATP or dithiothreitol. Since dithiothreitol restores the activity of (Na+ + K+)-ATPase, which had previously been inactivated by this ATP analog, it is concluded that thionosine triphosphate disulfide reacts with a sulfhydryl group in the ATP binding site of (Na+ + K+)-activated ATPase.
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PMID:Disulfide of thionosine triphosphate, an ATP-analog inactivating (Na+ + K+)-ATPase. 12 99

Accelerated calcium transport into the sarcoplasmic reticulum (SR) of the heart may mediate the inotropic actions of agents that act to increase adenosine 3',5'-monophosphate (cyclic AMP) within the cell. Studies in our laboratory have shown that ATP-dependent Ca uptake by cardiac microsomes rich in SR is enhanced by pretreatment with bovine cardiac cyclic AMP-dependent protein kinase (cyclic AMP-PK). Ca2+-activated ATPase is increased concomitantly with Ca uptake, stoichiometric coupling of 2 moles of Ca2+ taken up per mole of ATP hydrolyzed remaining constant. The steady state level of Ca binding is not increased by cyclic AMP-PK pretreatment, suggesting that the turnover rate of the transport system rather than the number of transport sites is increased. Phosphorylation of the SR by protein kinase is half-maximal at approximately 10(-7) M cyclic AMP, a value similar to that which gives half-maximal stimulation of both Ca uptake and Ca2+-activated ATPase. Over 80 percent of the 32P associated with membrane protein is identifiable as phosphoserine and phosphothreonine. The 32P is incorporated into a 22,000-dalton protein as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This protein, which we have tentatively named phospholamban (lambda alpha mu beta alpha psi usilon epsilon omega = to receive) appears to particiapte in the regulation of calcium transport by the heart's SR and may play a role in the inotropic actions of drugs, such as epinephrine, which act upon the cyclic AMP-PK system.
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PMID:Phospholamban: a regulatory protein of the cardiac sarcoplasmic reticulum. 12 51


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