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At least 739 records · Page 41Linked to original sources
PubMed1980

Adenosine triphosphatase activity and its sensitivity to ruthenium red oscillate during the cell cycle of Escherichia coli K12.

A procedure has been developed for the large-scale fractionation into size and age classes of bacteria from exponentially growing cultures of Escherichia coli K12 by centrifugation through an equivolumetric gradient of sucrose in a zonal rotor. The resolution attained is superior to that in methods of this type that have been described previously. The activity of adenosine triphosphatase (ATPase) was assayed in extracts from bacteria separated into size classes by this method and from synchronous cultures prepared by size selection. Activity approximately doubled during a cell cycle, but the experimental data did not fit models of either continuously or exponentially increasing activity during the cycle. It is suggested that ATPase activity oscillates during the cell cycle with maxima at about 0.37 and 0.80 of a cycle. The fluctuations in activity greatly exceed the variations due to experimental error and, in the case of synchronous cultures, do not arise from perturbations in growth behaviour following zonal gradient selection. Sensitivity of ATPase activity to 75 micrometer-Ruthenium Red also fluctuates during the cell cycle, with maximum inhibition (60 to 80%) occurring near the middle of the cycle, a time that does not coincide with maximum enzyme activity.

Adenosine Triphosphatases↗
PubMed1977

Effects of DDT on eggshell quality and calcium adenosine triphosphatase.

Adult mallard ducks were fed a diet containing 50 ppm DDT for 6 months. Eggs laid during this period were collected and eggshell weight, thickness, and calcium were determined. Chronic ingestion of DDT resulted in production of eggshells that were significantly thinner and lighter than those of controls. Total calcium of thinned eggshells was also reduced; however, calcium per gram of eggshell was not altered, indicating that other eggshell constituents were not incorporated as well. Calcium adenosine triphosphatase activity in the microsomal fraction of eggshell gland epithelium was assayed in control and DDT-fed ducks. Enzyme activity in DDT-fed ducks was reduced to 65% of control values. Since Ca-ATPase has been shown to be associated with calcium transport, enzyme inhibition may be responsible for decreased eggshell weight and thickness. Electron microscopic evaluation of microsomal fractions showed elements of the plasma membrane, including cilia and microvilli, as well as rough and smooth endoplasmic reticulum. Inhibition of calcium transport at the plasma membrane of mucosal epithelium is proposed as a possible mechanism of DDT-induced eggshell thinning.

Adenosine Triphosphatases↗
PubMed1980

Subunits of the adenosine triphosphatase complex translated in vitro from the Escherichia coli unc operon.

The unc operon of Escherichia coli was split into two fragments by the restriction endonuclease HindIII. The operator-proximal portion was cloned into plasmid pACYC184, forming plasmid pAN51, which included the genes uncB, uncE, and uncA. When plasmid pAN51 was used as template in an in vitro transcription/translation system, the alpha subunit (from the uncA gene) and delta subunit of the F(1) adenosine triphosphatase (ATPase) were formed. In addition, three polypeptides of molecular weights 18,000, 17,000, and 14,000 were formed, and the significance of these polypeptides is discussed. The operator-distal portion of the unc operon was also cloned into plasmid pACYC184, forming plasmid pAN36, which included the uncD and uncC genes. When this plasmid was used as template in an in vitro transcription/translation system, the beta subunit (from the uncD gene) and the epsilon subunit (from the uncC gene) of the F(1) ATPase were formed. A polypeptide of a molecular weight similar to the epsilon subunit but of different net charge was also formed. Plasmid pAN45, carrying the complete unc operon, was isolated after digestion of a mixture of plasmids pAN51 and pAN36 with the restriction endonuclease HindIII and then religation with T4 deoxyribonucleic acid ligase. It was concluded that a HindIII restriction site occurred within the newly described uncG gene, which was shown, by complementation studies with Mu-induced mutants, to be located between the uncA and uncD genes to give the gene order uncBEAGDC. The uncG gene appears to code for the gamma subunit of the F(1) ATPase.

Adenosine Triphosphatases↗
PubMed1980

[Alkaline phosphatase activity in the placental labyrinth of the cat and problems of specific localization of transport adenosine triphosphatase. An ultrastructural study (author's transl)].

The ultrastructural localizations of alkaline phosphatase (ALPase) and of Na+-K+-dependent adenosine triphosphatase (Na+-K+-ATPase) were studied in the placental labyrinth of the cat during the last days of gestation. ALPase activity could be detected in the syncytiotrophoblast but was absent from maternal tissues. Enzyme activity was observed only along plasma membranes of microvilli and absorption tubules on the maternal surface of the syncytium and also on the podocytes-like cytoplasmic processes of the fetal face. The localization of the Na+-K+-ATPase activity as obtained with the method of Ernst was identical with that of ALPase. This activity was not very ouabaine sensitive or K+ dependent, but was almost completely inhibited by levamisole. The strong ALPase activity of the syncytiotrophoblast does not allow a specific detection of Na+-K+-ATPase. However, the localization of these enzymes activities on syncytiotrophoblast surfaces directly related to fetal and maternal capillaries could suggest that these surfaces are associated with transport mechanisms of the trophoblast.

Alkaline Phosphatase↗
PubMed1985

Choroid plexus Na+/K+-activated adenosine triphosphatase and cerebrospinal fluid formation.

The quantitative relationship between intraventricular fluid formation and choroid plexus Na+/K+-activated (transport) adenosine triphosphatase (ATPase) was studied in rabbit and dog by perfusing the ventricular system with a solution containing ouabain (10(-8) to 10(-3) M). The effect of ouabain in the same range of concentrations on ATPase activity was also measured by the release of inorganic orthophosphate from in vitro choroid plexus tissue. Normally, about 20 to 25% of ATPase activity in lateral ventricle plexus is Na+/K+-activated, and this component is almost completely inhibited by ouabain in a concentration of 10(-4) M. At this concentration, the rate of intraventricular cerebrospinal fluid (CSF) formation is decreased some 70 to 80% in dog and rabbit. The results of this study suggest that a portion of the intraventricular fluid formation is insensitive to cardiac glycoside inhibition and that either there are two different mechanisms responsible for choroid plexus fluid formation or there is a significant non-ATPase dependent extrachoroidal source of CSF.

Animals↗
PubMed1994

Effects of the conventional anticonvulsants, phenytoin, carbamazepine, and valproic acid, on sodium-potassium-adenosine triphosphatase in acute ischemic brain.

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.

Animals↗
PubMed1989

Adenosine triphosphatase in the uterus and duodenum of chicken hens during eggshell formation.

Plasma calcium concentration and uterine and duodenal adenosine triphosphatase (ATPase) activities were determined during shell formation for high (H) and low (L) shell strength lines of hens selected from the last of four consecutive generations. The H and L lines were divided into three groups according to shell formation at 0, 15, and 22 h following oviposition. Plasma total calcium was determined from blood samples collected from the common carotid artery. Activity of ATPase was determined in uterine and duodenal mucosa. Shell strength, shell weight, percentage of shell per egg and shell thickness of the H line hens significantly exceeded those of the L line. During shell formation, no significant fluctuation in plasma calcium levels was observed within a line, but overall mean plasma calcium concentrations were higher in the H line than L line. Uterine ATPase activity increased with time after oviposition in both lines, with that of the H line being greater. Duodenal ATPase activity of H line hens remained fairly constant throughout the period, but this value showed fluctuations in the L line hens. It thus appears that laying hens with high and low shell strength may vary in their ability to use calcium for shell formation.

Animals↗
PubMed1979

Biosynthesis of the Ca2+- and Mg2+-dependent adenosine triphosphatase of sarcoplasmic reticulum in cell cultures of embryonic chick heart.

The biosynthesis of the Ca2+- and Mg2+-dependent adenosine triphosphatase of sarcoplasmic reticulum was studied in cell cultures of embryonic chick heart. Rates of synthesis were estimated from the incorporation of tritium-labeled leucine into the ATPase. Newly synthesized ATPase was isolated from cells by immunoprecipitation. Radioactive leucine incorporation into the ATPase was determined by gel electrophoresis of the immunoprecipitates and counting of gel slices containing the ATPase band. Accumulation of the ATPase was estimated from the concentration of Ca2+ and Mg2+-dependent, hydroxylamine-sensitive phosphoprotein in the whole cell membrane fraction of cultured cells. Embryonic heart cells cultured in a medium which permitted cell proliferation showed approximately linearly increasing rates of ATPase synthesis and accumulation/culture plate as the cells proliferated. When cells were cultured in a serum-free medium, cell proliferation was inhibited and there was no sustained increase in the rate of ATPase synthesis or accumulation. Inclusion of isoproterenol or dibutyryl cyclic AMP at concentrations of 10 microM up to 1 mM in serum-free culture medium failed to stimulate significantly ATPase synthesis.

Animals↗
PubMedDate not supplied

Changes in sarcolemmal adenosine triphosphatase activity and in ouabain sensitivity of rat myocardium in isoproterenol-induced cardiac hypertrophy.

Sodium, potassium-activated adenosine triphosphatase (ATPase) activity and the sensitivity of rat myocardium to ouabain was studied in isoproterenol (IPR)-induced cardiac hypertrophy. IPR in a dose of 5 mg/kg was administered to rats intraperitoneally, once daily, for seven days. Left ventricular trabeculae originating from IPR-treated rats were significantly less sensitive than controls to ouabain-induced positive inotropy. In crude homogenate and sarcolemmal fractions the ATP hydrolysing activity both in the presence of Mg++ (basic) and Mg++, Na+, K+ (total) was significantly reduced in the heart of IPR-treated rats. The difference between the total and basic ATPase, i.e. the Na+, K(+)-stimulated portion of the activity was slightly reduced, but the sensitivity of Na+, K(+)-ATPase to ouabain remained unchanged. The results indicate that the well-known relation of sodium pump inhibition to positive inotropy in the heart of IPR-treated rats may not be valid.

Animals↗
PubMed1986

Renal Na,K-adenosine triphosphatase transport rate limits transcellular NaCl reabsorption in distal nephrons of volume-expanded dogs.

To examine whether the adenosine triphosphatase (Na,K-ATPase) transport rate regulates transcellular NaCl reabsorption, experiments were performed on anesthetized volume-expanded dogs. Ouabain was injected into the renal artery in doses inhibiting 10 to 80% of the renal Na,K-ATPase activity. Acetazolamide was administered before ouabain to render the NaHCO3 reabsorption and associated NaCl reabsorption constant during variations in the glomerular filtration rate. Ouabain reduced sodium reabsorption significantly after inhibiting 20% of the Na,K-ATPase. By inhibiting 80% of the Na,K-ATPase, NaCl reabsorption was reduced by 40 to 50% without affecting NaHCO3 reabsorption. During mechanical constriction of the suprarenal aorta, the remaining NaCl reabsorption was constant until the glomerular filtration rate was lowered by about 50%. Bound ouabain and the remaining Na,K-ATPase activity were distributed between the cortex and medulla in proportion to the Na,K-ATPase activity before ouabain injection. The reduction in NaCl reabsorption and ouabain binding were correlated (r = 0.90), the slope suggesting a turnover for ATP similar to the in vitro turnover of 5700 ATP min-1 estimated from the relationship between the remaining Na,K-ATPase activity and bound ouabain (r = 0.95). We conclude that transcellular reabsorption of NaCl in the distal nephron reaches a maximum in volume-expanded dogs by saturating the sodium sites of Na,K-ATPase because even a small dose of ouabain inhibits NaCl reabsorption and because the calculated turnover for Na,K-ATPase activity is similar to in vitro maximum estimates. The Na,K-ATPase transport rate, therefore, limits transcellular NaCl reabsorption in volume-expanded dogs.

Absorption↗