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At least 217 records · Page 12Linked to original sources
PubMed1965

Adenosine-triphosphatase activity and nicotinamide nucleotide coenzymes in the parotid gland of the young lamb and adult sheep.

1. The activity of a Mg(2+)-dependent Na(+)-plus-K(+)-activated adenosine triphosphatase and the concentrations of nicotinamide nucleotide coenzymes have been measured in the immature parotid glands of young lambs and in the actively secreting glands of adult sheep. 2. The activity of the adenosine triphosphatase increased during development and attained relatively high levels in the mature secreting gland. 3. A high ([NAD]+[NADH(2)])/([NADP]+[NADPH(2)]) ratio (approx. 10:1) was observed in the parotid glands of lambs and sheep. 4. The high concentrations of NAD and the very low concentrations of NADPH(2) have been discussed in relation to metabolic activity, the activity of the Na(+)-plus-K(+)-activated adenosine triphosphatase and the secretion of saliva by the parotid gland.

Journal Article↗
PubMed1989

Parietal cell antibodies in pernicious anemia inhibit H+, K+-adenosine triphosphatase, the proton pump of the stomach.

Antibodies to a membrane-bound antigen, localized to the canalicular structures of the parietal cell, are found in most sera of patients with chronic atrophic gastritis and pernicious anemia. In the present study immunoglobulins containing parietal cell antibodies were found to inhibit the activity of H+,K+-adenosine triphosphatase (EC 3.6.1.36) in a tubulovesicular membrane preparation from porcine gastric mucosa. The degree of inhibition correlated to the titer of parietal cell antibodies as assessed by an enzyme-linked immunosorbent assay. The specificity of the enzymatic inhibition was confirmed by the lack of effect of parietal cell antibodies on membrane-bound esterase. A possible interaction of parietal cell antibodies with gastrin binding at the receptor level was investigated in a radioreceptor assay employing 125I-gastrin 1 and gastric mucosal cell suspension from the guinea pig. No blocking capacity was found with immunoglobulins from patients with pernicious anemia as compared with immunoglobulins from healthy controls. The results thus demonstrate a direct inhibitory effect of parietal cell antibodies on the acid producing H+,K+-adenosine triphosphatase of the parietal cell, but also a lack of interaction with the gastrin receptor, and indicate that in the development of hypo/achylia H+,K+-adenosine triphosphatase autoantibodies could have a major pathogenic role.

Adenosine Triphosphatases↗
PubMed1994

Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins.

Bafilomycin A1, an inhibitor of vacuolar adenosine triphosphatase, was tested for its ability to antagonize botulinum neurotoxins (serotypes A-G), tetanus toxin and phospholipase A2 neurotoxins (notexin, beta-bungarotoxin, taipoxin and textilotoxin) on the mouse phrenic nerve-hemidiaphragm preparation. Bafilomycin itself produced concentration-dependent blockade of neuromuscular transmission without blocking nerve action potentials or muscle action potentials. This effect may have been due to inhibition of the proton pump that regulates acetylcholine transport into vesicles. At submaximal concentrations, bafilomycin was very effective in delaying the onset of paralysis due to all clostridial neurotoxins, but it had no protective effect against phospholipase A2 neurotoxins. Experiments were done to determine which of the three steps in clostridial neurotoxin action was antagonized by bafilomycin (e.g., binding, internalization and intracellular poisoning). Both pharmacological experiments and ligand-binding experiments showed that the drug did not block toxin binding to the plasma membrane. Similarly, pharmacological experiments on the time-dependent effects of bafilomycin showed that the drug did not antagonize the intracellular actions of toxins. The data indicated that bafilomycin acted at the intermediate step of internalization. This is in keeping with the facts that: 1) bafilomycin inhibits vacuolar adenosine triphosphatase, which in turn leads to inhibition of acidification in endosomes and 2) clostridial neurotoxins depend upon acidification of endosomes for translocation to the cytosol. The finding that bafilomycin antagonizes tetanus toxin may provide important clues for understanding how this toxin can act locally to produce flaccid paralysis. The finding that bafilomycin is a universal antagonist that protects against all clostridial neurotoxins may have important implications for developing therapeutic drugs.

Adenosine Triphosphatases↗
PubMed1980

Nucleotide binding to isolated alpha and beta subunits of proton translocating adenosine triphosphatase studied with circular dichroism.

The catalytic and allosteric sites of proton translocating adenosine triphosphatase (ATPase) were studied by measuring the binding of nucleotides to the ATPase, and its alpha and beta subunits purified from thermophilic bacterium PS3, with a circular dichroic spectrometer. In contrast to mesophilic ATPases, this thermophilic enzmye contained no tightly bound nucleotides, and its subunits were stable after their purification. These properties were advantageous for analyzing both catalytic and allosteric sites. The former site showed rapid and loose binding, but the latter slow (t 1/2 = 1 h, for ADP) and tight binding. When a nucleotide was bound, the beta subunits showed a negative ellipticity at 275 nm corresponding to a tyrosyl residue, while the alpha subunits showed an ellipticity change corresponding to the absorption curve of the bound nucleotide. This difference enabled us to distinguish the binding sites in ATPase. At a low concentration, ADP selectively bound to alpha subunits in the ATPase, while at a high concentration, it bound to both subunits. This finding suggests that the tight binding sites are located in the alpha subunits. Although ADP and ATP bound to both the purified alpha and beta subunits, CTP did not bind to beta but only to alpha subunits, and ITP bound to beta but hardly to alpha. These nucleotide specificities also supported the idea that the catalytic sites are located in the beta subunits and the allosteric sites are located in the alpha subunits.

Adenosine Diphosphate↗
PubMed1979

Solubilization of adenosine triphosphatase from membranes of Escherichia coli: effect of p-aminobenzamidine.

The five subunits of the membrane-bound adenosine triphosphatase (F1) from Escherichia coli were identified on electrophoretograms of membranes which had been washed with a low-ionic-strength buffer containing the protease inhibitor p-aminobenzamidine. All of the subunits of the membrane-bound F1 appeared to have the same molecular weights and isoelectric points as those of the soluble F1, as judged by two-dimensional electrophoresis. p-Aminobenzamidine inhibited the solubilization of F1 rebound to F1-depleted membranes, and was found to inhibit the membrane-bound adenosine triphosphatase activity to a much greater extent than the solubilized activity. It is therefore unlikely that p-aminobenzamidine inhibits the solubilization of F1 by inhibiting a protease, as suggested previously by Cox et al. (G.B. Cox, J.A. Downie, D.R.H. Fayle, F. Gibson, and J. Radik, J. Bacteriol. 133:287--292, 1978).

Adenosine Triphosphatases↗
PubMed1975

A Mg2+- and Ca2+-stimulated adenosine triphosphatase at the outer surface of Ehrlich ascites tumor cells.

A Mg2+- and Ca2+-stimulated adenosine triphosphatase (ATPase) at the outer surface of intact Ehrlich ascites tumor cells is described. A surface-bound adenosine triphosphate (ATP)-splitting activity at a lower rate was also demonstrated in the absence of Ca2+ but with Mg2+, Na+, and K+ present in the isotonic medium. Hence, when part of the Mg2+ was exchanged for Ca2+, a marked increase of the ATP-splitting activity was observed. The stimulatory effect of Ca2+ was seen only if both Na+ and K+ were present in the isotonic incubation medium. Thus, the enzyme activity was Mg2+- and Ca2+-dependent. Ca2+, together with the monovalent cations was inhibitory compared with Mg2+ under similar conditions. The apparent Km for ATP for the Mg2+-stimulated ATPase is 0.05 mM, while that of the Mg2+- and Ca2+-stimulated enzyme is 0.10 mM. The Vmax of the former is 0.8 mu-mole per 100 mg Schneider protein per 30 sec compared with 1.92 mu-moles per 100 mg Schneider protein per 30 sec for the latter. The calculated Km for the Mg2+- and Ca2+-stimulated ATPase after subtraction of the Mg2+-stimulated part is 0.22 mM. Ethacrynic acid and N-ethylmaleimide both inhibited the Mg2+- and Ca2+-stimulated ATPase by about 10 percent, while the ouabain inhibition was 15 percent. Cytochalasin B did not influence the enzyme activity, whereas La3+ had a slight stimulatory effect.

Adenosine Triphosphatases↗
PubMed1969

Adenosine triphosphatase. Sensitive to DDT in synapses of rat brain.

The insecticide DDT selectively inhibits the action of a Na(+), K(+), Mg(2+)-adenosine triphosphatase found in the nerve ending fraction of the rat brain. As judged by the concentrations of inhibitors that give 50 percent of enzyme inhibition, DDT was approximately 1000 times more toxic than its non-insecticidal analog, 1,1-dichloro-2,2-bis(p-chlorophenyl)ethylene. The degrees of inhibition of this enzyme system by various toxic and nontoxic DDT analogs were closely related to a general toxicity in vivo of these compounds. Moreover, the extents of inhibition of this enzyme system by DDT were much higher at low temperatures, an indication of a causal relation between poisoning in vivo by DDT and the inhibition in vitro of the Na(+), K(+), Mg(2+)-adenosine triphosphatase system.

Adenosine Triphosphatases↗
PubMed1978

Characterization of the mutant-unc D-gene product in a strain of Escherichia coli K12. An altered beta-subunit of the magnesium ion-stimulated adenosine triphosphatase.

Membranes from a mutant strain of Escherichia coli K12 carrying the uncD409 allele were washed in low-ionic-strength buffers in the presence or absence of the proteinase inhibitor p-aminobenzamidine. Unlike membranes from a normal strain, those from strain AN463 (uncD409) did not become proton-permeable, as judged by NADH-induced atebrinfluorescence quenching, when the membranes were washed in the absence of p-aminobenzamide. Furthermore, ATP-dependent atebrin-fluorscence quenching in such washed membranes could not be reconstituted by the addition of solubilized Mg2+-stimulated adenosine triphosphatase preparations. The examination by two-dimensional polyacrylamide-gel electrophoresis of the polypeptide composition of the washed membranes from strain AN463 (uncD409) indicated the presence of a polypeptide of similar molecular weight to the normal beta-subunit of the Mg2+-stimulated adenosine triphosphatase, but with an altered isoelectric point. Both the normal and abnormal beta-subunits were identified in membranes prepared from a partial diploid strain carrying both the unc+ and uncD409 alleles. It is concluded that the uncD gene codes for the beta-subunit of the Mg2+-stimulated adenosine triphosphatase.

Adenosine Triphosphatases↗
PubMed1979

The uncA gene codes for the alpha-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains.

Four mutant strains of Escherichia coli which lack membrane-bound adenosine triphosphatase activity were shown by genetic-complementation tests to carry mutations in the uncA gene. A soluble inactive F1-ATPase aggregate was released from the membranes of three of the uncA mutant strains by low-ionic-strength washing, and purified by procedures developed for the purification of F1-ATPase from normal strains. Analysis of the subunit structure by two-dimensional gel electrophoresis indicated that the F1-ATPase in strains carrying the uncA401 or uncA453 alleles had a subunit structure indistinguishable from normal F1-ATPase. In contrast, the F1-ATPase from the strain carrying the uncA447 allele contained an alpha-subunit of normal molecular weight, but abnormal net charge. Membranes from strains carrying the uncA450 allele did not have F1-ATPase aggregates that could be solubilized by low-ionic-strength washing. However, a partial dipolid strain carrying both the uncA+ and uncA450 alleles formed an active F1-ATPase aggregate which could be solubilized by low-ionic-strength washing of the membranes and which contained two types of alpha-subunit, one of which was normal and the other had abnormal net charge. It is concluded that the uncA gene codes for the alpha-subunit of the adenosine triphosphatase.

Adenosine Triphosphatases↗
PubMed1977

Erythrocyte cation-activated adenosine triphosphatases in Duchenne muscular dystrophy.

The cation-stimulated adenosine triphosphatase (ATPase) activities of erythrocyte ghosts and erythrocyte ghost plasma membrane fragments of patients with Duchenne muscular dystrophy (DMD) were compared with activities in age-matched normal male controls. DMD Mg++-stimulated ATPase activity was within the normal range. The specific activity of DMD erythrocyte ghost Na+,K+-stimulated, Mg++-dependent ATPase was also normal, and was inhibited by 10(-4) M ouabain to an extent comparable with controls. Ca++-stimulated, Mg++-dependent ATPase activity of DMD erythrocyte ghost plasma membrane fragments, assayed at 0.5 mM free Ca++, was 21% above that in age-matched male controls (n = 22, 2-tailed paired t-test, P less than 0.01). Kinetic studies indicated that the DMD erythrocyte Ca++-stimulated, Mg++-dependent ATPase has greater affinity for MgATP than the enzyme in control erythrocytes.

Adenosine Triphosphatases↗
PubMed1980

Lack of 'acid reversal' of myofibrillar adenosine triphosphatase in masticatory muscle fibres of rhesus monkeys.

Myofibrillar adenosine triphosphatase (ATPase) activity was demonstrated in sections of masseter and temporalis muscles and of selected limb muscles of adult rhesus monkeys. Incubations were performed either with no pre-treatment or after prior incubation in alkaline media (pH 10.2-10.4) or acidic media (pH 3.8-4.6). Without pre-treatment, fibres having high or low ATPase activity were observed in limb and masticatory muscles. Following alkaline pre-incubation the difference between high and low ATPase of limb muscle fibres is accentuated, whereas pre-incubation in acidic media (pH 4.3) results in inhibition of high and potentiation of low ATPase activities ('acid reversal'). While pre-incubation of masticatory muscle sections at pH 10.2 accentuates differences in ATPase activity, pre-incubation at pH 10.4 abolishes ATPase activity. In contrast, masticatory muscle fibres showed no reversal of ATPase activity following acidic pre-incubation (pH 4.3). Pre-incubation at pH 3.8 abolished the ATPase activity of both limb and masticatory muscle fibres. The biochemical basis for the differences in ATPase histochemistry between masticatory and limb muscles is not known.

Adenosine Triphosphatases↗
PubMed1980

Na,K-, Mg- and HCO3-adenosine triphosphatases in the rabbit brain choroid plexus.

Properties of adenosine triphosphatases (ATPases) in the choroid plexus of rabbit cerebral ventricles were investigated using tissue homogenates and subcellular fractions. Na,K-ATPase or HCO3-ATPase activity of choroid plexus was significantly lower than that of the brain or the kidney, respectively. Among the homogenates of choroid plexus from the lateral, third and fourth ventricles, there were no differences in the activities of Na,K-, Mg- and HCO3-ATPases. In the choroid plexus, Na,K-ATPase activity was demonstrated to be highest in 10,000 X g fraction, while the highest Mg- and HCO3-ATPase activities were observed in 8,000 X g fraction, the so-called mitochondrial fraction. Ion requirement, pH optimum and ouabain sensitivity of Na,K-ATPase in 10,000 X g fraction of choroid plexus were similar to findings in erythrocytes, brain and kidney. However, properties of Mg- and HCO3-ATPases in 8,000 X g fraction were considerably different from those found in the brain and gastric mucosa. In the choroid plexus, thiocyanate ion inhibited Mg-ATPase as well as HCO3-ATPase. These results indicate that characteristics of ATPase systems in the choroid plexus are to some extent different from those in tissues such as brain, kidney and gastric mucosa.

Adenosine Triphosphatases↗