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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phosphatase activity in Trypanosoma rhodesiense has been examined histochemically by light and electron microscopy and by enzymatic assay in homogenate fractions. Using a method with lead as capture ion, acid phosphatase was found in lysosome-like vesicles and in the flagellar pocket. No alkaline adenosine triphosphatase (ATPase) was detectable by this method. Direct assay of p-nitrophenylphosphatase activity in homogenate fractions showed that acid phosphatase activity was strongly membrane-bound, but that activity at pH 9 was minimal in both soluble and particulate fractions. "Endogenous" ATPase activity was localized specifically and reproducibly in the mitochondrial membranes and under the plasma membrane of he flagellum. This nonenzymic reaction product could not be eradicated by glycerol extraction or glucose depletion. Unlike the membrane staining, which was manifest only after lead treatment, heat-resistant electron-dense material was found in the matrix of lysosomal vesicles in trypanosomes fixed in glutaraldehyde only and not subjected to further treatment with heavy metal reagents. X-ray emission analysis showed the presence of calcium and phosphorus, indicating that the matrix might have a phosphate storage function.
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PMID:Localization of phosphatases in Trypanosoma rhodesiense. 645 52

During growth and maturation of the tapeworm, Hymenolepis diminuta, significant decreases occur in the brush border membrane-bound alkaline phosphatase, phosphodiesterase, 5'-nucleotidase, adenosine triphosphatase and ribonuclease activities. These decreases are accompanied by qualitative and quantitative changes in the polypeptide profiles of the brush border membrane fraction. Gradients of enzymatic activities and polypeptide profiles are also demonstrable when mature tapeworms are cut into pieces and the brush border membrane of each piece analyzed individually. In fully developed tapeworms the enzymatic activities and polypeptide profiles of membrane preparations reflect mainly the contributions of the more mature proglottids; these proglottids constitute most of the tapeworm biomass. The most anterior sections of these fully developed worms are biochemically similar to young, developing worms.
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PMID:Alterations in brush border membrane proteins and membrane-bound enzymes of the tapeworm, Hymenolepis diminuta, during development in the definitive host. 663 65

Experiments with the aerotolerant anaerobe Streptococcus lactis provide the opportunity for determining the proton motive force (Deltap) in dividing cells. The two components of Deltap, DeltaPsi (the transmembrane potential) and DeltapH (the chemical gradient of H(+)), were determined by the accumulation of radiolabeled tetraphenylphosphonium (TPP(+)) and benzoate ions. The DeltaPsi was calibrated with the K(+) diffusion potential in starved, valinomycin-treated cells. With resting, glycolyzing cells, the Deltap was measured also by the accumulation of the non-metabolizable sugar thiomethyl-beta-galactoside (TMG). In resting cells the Deltap, calculated either by adding DeltaPsi and ZDeltapH or from the levels of TMG, was relatively constant between pH 5 to 7, decreasing from 160 to 150 mV and decreasing further to 100 mV at pH 8.0. With the TPP(+) probe for DeltaPsi, we confirmed our previous finding that the K(+) ions dissipate DeltaPsi and increase DeltapH, whereas Na(+) ions have little effect on DeltaPsi and no effect on DeltapH. [(3)H]TPP(+) and [(14)C]benzoate were added during exponential phase to S. lactis cells growing at pH 5 to 7 at 28 degrees C in a defined medium with glucose as energy source. As with resting cells, the DeltapH and DeltaPsi were dependent on the pH of the medium. At pH 5.1, the DeltapH was equivalent to 60 mV (alkaline inside) and decreased to 25 mV at pH 6.8. The DeltaPsi increased from 83 mV (negative inside) at pH 5.1 to 108 mV at pH 6.8. The Deltap, therefore, was fairly constant between pH 5 and 7, decreasing from 143 to 133 mV. The values for Deltap in growing cells, just as in resting cells, are consistent with a system in which the net efflux of H(+) ions is effected by a membrane-bound adenosine triphosphatase and glycolytically generated adenosine triphosphate. The data suggest that in both growing and resting cells the pH of the medium and its K(+) concentration are the two principal factors that determine the relative contribution of DeltapH and DeltaPsi to the proton motive force.
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PMID:Proton motive force during growth of Streptococcus lactis cells. 677 26

Attachment values of Mycoplasma pneumoniae to glass are normally very low when tested in buffer containing bovine serum albumin (10 mg/ml). However, the addition of one of the metabolizable sugars glucose, fructose, or mannose increased attachment more than 10-fold. The effect was dose dependent with a distinct optimum at about 0.25 mg/ml. Higher concentrations reduced this effect. Not only the sugars themselves but also the products of their catabolism, pyruvate and phosphoenolpyruvate, enhanced attachment. Pyruvate was effective in the same range of concentrations as the sugars, whereas phosphoenolpyruvate enhanced attachment at a significantly lower concentration (0.001 mg/ml). Higher levels of these substances also resulted in a decrease of attachment. The glucose-induced increase could be partially inhibited by glucose analogs, especially by 3-O-methyl-glucopyranoside, and by various inhibitors or glycolysis. Furthermore, attachment was strongly reduced by the uncoupling agents carbonylcyanide m-chlorophenylhydrazone and 2,4-dinitrophenol, as well as by dicyclohexylcarbodiimide, an inhibitor of the membrane-bound Mg2+-adenosine triphosphatase, whereas the ionophore valinomycin increased attachment by about 30%. These findings provide strong evidence for coupling between the attachment process of M. pneumoniae to glass and the utilization of metabolic energy.
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PMID:Role of energy metabolism in Mycoplasma pneumoniae attachment to glass surfaces. 678 36

The electrochemical proton gradient across mycoplasmal membranes was studied. The transmembrane proton-motive potential, delta p, is composed of two parameters, a transmembrane electric potential difference, delta psi, and a transmembrane proton gradient, delta pH, according to the formula delta p = delta psi -(A x delta pH). Membrane potentials were determined with use of potential-sensitive cyanine dyes. The delta psi for both Mycoplasma mycoides subspecies capri and Mycoplasma gallisepticum was -48 mV +/- 10%, with the inside negative; the delta psi of Acholeplasma laidlawii was -28mV +/- 20%. The delta pH was determined by measuring the distribution of [14C]5,5-dimethyl oxazolidine-2,4-dione between the intracellular space and the medium. The intracellular pH of glycolyzing mycoplasmas was generally more alkaline than the extracellular medium: at an external pH of 7.0, the internal pH was 7.4 and hence delta pH = 0.4, a value corresponding to -24 mV. Thus, the delta p of both M. mycoides subspecies capri and M. gallisepticum was calculated to be -72 mV and that of A. laidlawii, to be -52 mV. The data further indicate that the delta p is generated by a membrane-bound electrogenic, proton-translocating adenosine triphosphatase that operates in the direction of hydrolysis of adenosine triphosphatase, which formed by glycolysis, and leads to proton extrusion.
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PMID:The electrochemical potential across mycoplasmal membranes. 712 58

A radiation inactivation technique was employed to determine the functional size of adenosine triphosphatase from Escherichia coli (EF0EF1-ATPase). Functional units of the membrane-bound and the soluble ATPases were estimated to be 300 +/- 39 and 295 +/- 32 kDa, respectively. The presence of the free radical scavenger dithiothreitol was crucial in measuring the radiation inactivation size of ATPase. When gramicidin and carbonyl cyanide p-trifluoromethoxyphenylhydrazone were added, an increase in the functional mass of membrane-bound ATPase was observed. In contrast, valinomycin and KCl had hardly any effect on the functional size of ATPase. We also determined a functional unit of 355 +/- 33 kDa for proton translocation by a fluorescence quenching technique. A reconstitution study using irradiated coupling factor 1 (EF1)-depleted membrane revealed that the functional mass of the proton channel was 96 +/- 11 kDa. A similar functional size for ATP-Pi exchange and ATP hydrolysis implies that both reactions might utilize identical machinery. Furthermore, functional units of soluble EF1 for unisite (nonsteady state) and multisite (steady state) ATP hydrolysis were calculated as 200 +/- 32 and 298 +/- 32 kDa, respectively. A working hypothesis was proposed from radiation inactivation analysis to elucidate the structure and mechanism of F1-ATPase.
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PMID:Functional size analysis of F-ATPase from Escherichia coli by radiation inactivation. 768 67

Physical-chemical-activity relationship of aromatic hydrocarbons (n = 10) and alkyl acetates (n = 16) with respect to their in vitro effects on synaptosomal membranes was studied. Na(+)-K(+)-adenosine triphosphatase (Na(+)-K(+)-ATPase) activity and membrane fluidity, which was determined using the fluorescence probe 1,6-diphenyl-1,3,5-hexatriene, were used as potential indicators of neuronal cell toxicity. The potency of inhibition for the enzyme (IC50), the potency of increasing membrane fluidity (IC12.5), and n-octanol/water partition coefficient (P) were all determined experimentally for 26 solvents. Correlation analyses were made on aromatic hydrocarbons and on alkyl acetates. There were linear relationships between log P and pIC50 (log1/IC50) values, and between log P and pIC12.5 (log1/IC12.5) values, indicating that the hydrophobicity of the solvents determines their toxic ability to affect membrane environment; the more hydrophobic the solvents are, the more toxic they are. A direct linear relationship between Na(+)-K(+)-ATPase activity pIC50 and membrane fluidity pIC12.5 values was also shown. This predictive correlation suggests a similar mechanism of membrane surface interaction govering both processes that are common to the test solvents. The present results confirm the importance of the lipid environment of neuronal membranes in maintaining the normal function of membrane-bound protein.
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PMID:Physical-chemical-activity relationship of organic solvents: effects on Na(+)-K(+)-ATPase activity and membrane fluidity in mouse synaptosomes. 786 56

The localization of some membrane-associated enzymes such as alkaline phosphatase, 5'-nucleotidase, glucose-6-phosphatase, Na+,K(+)-adenosine triphosphatase, adenylate cyclase and guanylate cyclase in the Merkel cell-axon complexes, trigeminal ganglia and the principal trigeminal sensory nucleus of the cat was determined at light and electron microscopic level using cytochemical techniques. In the sinus hair follicles (vibrissae), the reaction end product marking alkaline phosphatase and adenosine triphosphatase activities was visualized on the axons running through external follicle epithelium and the 5'-nucleotidase, adenylate- and guanylate cyclase positive reaction was seen to stain the plasma membranes of Merkel cells. In the trigeminal ganglia, the strongest alkaline phosphatase and adenosine triphosphatase activities showed the corresponding areas between the ganglion and satellite cells. 5'-nucleotidase activity was more intense on the neurilemmas and the surrounding glial plasma membranes. In the principle sensory trigeminal nucleus, the central neurons exhibited an intense alkaline phosphatase, 5'-nucleotidase and adenosine triphosphatase activities and much smaller amount of reaction product for adenylate cyclase and guanylate cyclase was observed. In conclusion, membrane-bound enzymes could be histo- and cytochemically demonstrated in all components of primary trigeminal afferent units. Our results have confirmed that the receptor function and the nerve impulses conductance need an intensive molecular and cation exchange, and energy supply.
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PMID:Primary trigeminal afferent neuron of the cat: I. Studies on membrane-bound enzyme histochemistry. 798 69

The effects of phenytoin, carbamazepine and valproic acid on alterations in sodium-potassium-adenosine triphosphatase activity during ischemia were studied in the rat brain. Pretreatment with phenytoin and carbamazepine prevented a reduction of this activity, which, without either treatment, was observed in the cerebral hemisphere exposed to 30-minute ischemia resulting from unilateral middle cerebral artery occlusion. Valproic acid, on the other hand, did not principally affect the ischemic impairment of this membrane-bound enzyme activity. These results lend support to the previously proposed use of phenytoin in cerebral ischemia, but also suggest the therapeutic availability of another common anticonvulsant, carbamazepine, for treatment of the insult.
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PMID:Effects of the conventional anticonvulsants, phenytoin, carbamazepine, and valproic acid, on sodium-potassium-adenosine triphosphatase in acute ischemic brain. 808 89

The structure-toxicity relationship of monoketones, a class of organic solvents widely used in industry, was investigated with respect to their in vitro effects on synaptosomal membrane proteins. The toxic parameters used were Na(+)-K(+)-adenosine triphosphatase (Na(+)-K(+)-ATPase), a well-known marker enzyme often used as a membrane toxicity model, and 3H-dihydroalprenolol (3H-DHA)-labeled beta-adrenergic receptor binding that has been shown to be vulnerable to solvent-induced changes in membrane fluidity. In vitro treatments with 12 kinds of monoketones (carbon chain length from 3-10) dose-dependently inhibited both 3H-DHA binding to mouse synaptosomes and Na(+)-K(+)-ATPase activity. The potency of inhibition (IC50) for both the two parameters was linearly related to n-octanol/water partition coefficient and synaptosome/buffer partition coefficient of the test compounds. Additions of monoketones did not significantly alter the number of 3H-DHA binding sites but markedly decreased their affinity. In each monoketone, the IC50 values for 3H-DHA binding and Na(+)-K(+)-ATPase activity were generally within the same range. The anisotropy of fluorescence probe 1,6-diphenyl-1,3,5-hexatriene-labeled synaptosomal membranes was dose-dependently decreased by the monoketones, implying increased membrane fluidity. These results indicate that increasing lipophilicity of monoketones results in increased solvent penetration of synaptic membrane preparations, leading to conformational changes in membrane structure and increased ability to inhibit both neuroreceptor binding and enzyme activity. The present data confirm the importance of the lipid micro-environment of membranes in maintaining the normal functions of membrane-bound proteins.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Structure-toxicity relationship of monoketones: in vitro effects on beta-adrenergic receptor binding and Na(+)-K(+)-ATPase activity in mouse synaptosomes. 827 28


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