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 transverse distribution of enzyme proteins and phospholipids within microsomal membranes was studied by analyzing membrane composition after treatment with proteases and phospholipases. Upon trypsin treatment of closed microsomal vesicles, NADH- and NADPH-cytochrome c reductases as well as cytochrome b5 were solubilized or inactivated, while cytochrome P-450 was partially inactivated. When microsomes were exposed to a concentration of deoxycholate which makes them permeable to macromolecules but does not disrupt the membrane, the detergent alone was sufficient to release four enzymes: nucleoside diphosphatase, esterase, beta-glucuronidase, and a portion of the DT-diaphorase. Introduction of trypsin into the vesicle lumen inactivated glucose-6-phosphatase completely and cytochrome P-450 partially. The rest of this cytochrome, ATPase, AMPase, UDP-glucuronyltransferase, and the remaining 50% of DT-diaphorase activity were not affected by proteolysis from either side of the membrane. Phospholipase A treatment of intact microsomes in the presence of albumin hydrolyzed all of the phosphatidylethanolamine, phosphatidylserine, and 55% of the phosphatidylcholine. From this observation, it was concluded that these lipids are localized in the outer half of the bilayer of the microsomal membrane; Phosphatidylinositol, 45% of the phosphatidylcholine, and sphingomyelin are tentatively assigned to the inner half of this bilayer. It appears that the various enzyme proteins and phospholipids of the microsomal membrane display an asymmetric distribution in the transverse plane.
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PMID:Enzyme and phospholipid asymmetry in liver microsomal membranes. 19 Feb 41

One hour after a single i.v. dose of 250 mg/kg folic acid, the straight portion of distal tubules in the outer medulla of rat kidneys showed a distinct reduction in succinate dehydrogenase, NADH2-diaphorase, glutamate dehydrogenase, cytochrome oxydase, Na+/K+-ATPase, and acid phosphatase activity. In contrast, the proximal tubules exhibited only a reduction in glutamate dehydrogenase and alkaline phosphatase activity. At this time the straight portion of the distal tubules, whose enzyme activity had changed, showed partly regressive epithelial changes. 24 hours after folic acid administration an even greater reduction in enzyme activity had occurred in the straight portion of distal tubules; these structures also became dilated. The adjacent collecting tubules and the corresponding proximal tubules were also severely dilated, the proximal tubules showing a loss in enzyme acitivities similar to those observed in the distal tubules. 48 hours after folic acid administration the changes largely resembled those observed after 24 hours, but were more pronounced. At this time a tubular regeneration was observed. 72 hours after folic administration extensive normalization of the histological and histochemical changes had occured. It is postulated that a disturbance of the hairpin counter-current mechanism occurs as a result of a direct, concentration-dependent effect of folic acid on the enzymes of the energy supplying metabolism. A dilation in the region of the loop of Henle and the collecting tubules occurs subsequently.
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PMID:Enzyme histochemistry of rat folic acid nephropathy. 19 86

Post-tetanic potentiation (PTP) of monosynaptic reflex was estimated in spinal cords in the drug-free state after the administration of a convulsant dose of penicillin and after the administration of phenytoin. There was no apparent correlation between the degree of depression of PTP and the efficacy of controlling seizure activity by phenytoin. Extracellular potassium levels were measured with ion-selective microelectrodes. The post-stimulation clearing of [K+]0 was not accelerated by phenytoin, and frequently it was slowed. Post-stimulus undershooting of [K+]0 was diminished. Oxidation of NADH in cortex and of cytochrome a, a3 in spinal cord were measured by optical methods. Stimulus-evoked transient oxidation responses evoked by electrical stimulation were depressed by phenytoin. It is concluded that systemic administration of phenytoin in therapeutic doses does not stimulate Na+-K+-activated membrane ATPase in cortex and spinal cord. Unlike other depressants, phenytoin did not cause a reduction of "resting" redox levels of respiratory enzymes. The local regulation of blood flow remained unaltered after phenytoin administration. Phenytoin caused a moderate but consistent depression of the stimulus-evoked responses of potassium activity, electric potential, and oxidative enzymes, consistent with diminished outflow of potassium from cells, owing either to lesser activation of cells or to a lesser exchange of ions.
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PMID:Phenytoin, electric, ionic, and metabolic responses in cortex and spinal cord. 19 41

The content of cytochrome c-420 in Rhodospirillum rubrum chromatophores prepared by grinding with alumina is 5--10% of that in whole cells, and 20--40% in chromatophores by 'French' pressing. Flash-induced phosphorylation of various chromatophores which varied in cytochrome content from 7 to 40% is proportional to the cytochrome content. Extrapolating the cytochrome c-420 content to that observed in whole cells, a ratio ATP/P+X- near 1 is calculated. At low flash intensity the phosphorylation per flash is proportional to flash energy. Photophosphorylation in flashes given after a time of several minutes is only slightly dependent on the number of flashes. If the flashes are spaced from 0.1 to 10 s, relative phosphorylation in the first flash is about 70% and in the second 90+ of that observed in the following flashes. Proton binding is not affected by the cytochrome c-420 content and a ratio of H+/P+x- of 2.3 was found. These results can be explained by a working hypothesis in which charge separation occurring at one reaction centre and the resulting electron transport mediated amongst others by c-420, results in the injection of two protons into an ATPase, this in contrast to a chemiosmotic mechanism, where the protons are released in the chromatophore inner space.
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PMID:Flash-induced photophosphorylation in Rhodospirillum rubrum chromatophores. I. The relationship between cytochrome c-420 content and photophosphorylation. 21 10

The effects of vitamin E deficiency on membrane integrity were studied by examining the temperature dependence of membrane-bound enzyme activities in liver mitochondria and microsome and in muscle sarcoplasmic reticulum. In vitamin E-deficient rabbits, the specific activities at 37 degrees of mitochondrial oligomycin-sensitive ATPase (EC 3.6.1.3), beta-hydroxybutyrate dehydrogenase (EC 1.1.1.30), and microsomal glucose-6-phosphatase (EC 3.1.3.9) were increased, whereas those of microsomal NADH cytochrome C reductase (EC 1.6.99.3) and sarcoplasmic reticulum Ca-ATPase were reduced in comparison to control rabbits. Arrhenius plots of activity against temperature yielded a linear plot over the range 10 to 40 degrees in the case of beta-hydroxybutyrate dehydrogenase, NADH cytochrome C reductase and Ca-ATPase, and multiple discontinuities for glucose-6-phosphatase and oligomycin-sensitive ATPase. In control rabbits, all five enzymes showed a single discontinuity in the Arrhenius plot over the range 16 to 19 degrees. These results reflect changes in the microenvironment of membrane-bound enzymes as a consequence of vitamin E depletion.
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PMID:Effects of vitamin E deficiency on the activities of lipid-requiring enzymes in rabbit liver and muscle. 22 Mar 97

1. The sterol, unsaturated fatty acid and cytochrome contents of cells of a delta-aminolaevulinate synthase mutant of Saccharomyces cerevisiae are manipulated by growing the organism in media containing defined supplements of delta-aminolaevulinate and other porphyrin intermediates. 2. If unsaturated fatty acids are added to the growth medium as Tween 80, sterol content and respiratory cytochromes alone are manipulated. 3. In the presence of delta-aminolaevulinate (10-50mg/1) cells exhibit moderate to high respiratory activity, but growth yields are low, indicating a loss of oxidative phosphorylation. This is associated with the depletion of membrane lipids, either unsaturated fatty acids and sterols together or sterols alone. 4. Sterol depletion leads to the loss of coupled mitochondrial oxidative phosphorylation in vitro. 5. The lesion in oxidative phosphorylation is associated with an increase in the passive permeability of sterol-depleted mitochondria to protons. 6. Arrhenius plots of mitochondrial permeability to protons indicate that the activation energy for proton entry increases as the sterol content of the membranes decreases. 7. Studies on a cytoplasmic petite mutant isolated from strain ole-3, which lacks a functional membrane-bound protein-translocating adenosine triphosphatase, indicate that proton permeability of the petite mitochondria varies as a function of sterol composition in the same way as that of ole-3 grande mitochondria. This indicates that sterols alone are probably directly responsible for the increased proton entry, owing to a reorganization of the lipid in the membrane. 8. Supplemented ole-3 cells with a normal lipid composition and normal or higher than normal respiratory activities have a growth efficiency only 65% of that of the wild-type, indicating that a further lesion in energy metabolism may be present.
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PMID:The effects of altered membrane sterol composition on oxidative phosphorylation in a haem mutant of Saccharomyces cerevisiae. 33 62

Escherichia coli K-12, grown under anaerobic conditions with glucose as the sole source of carbon and energy without any terminal electron acceptor added, contains a fumarate reductase system in which electrons are transferred from formate or reduced nicotinamide adenine dinucleotide via menaquinone and cytochromes to fumarate reductase. This fumarate reductase system plays an important role in the metabolic energy supply of E. coli, grown under so-called "glycolytic conditions," as is indicated by the growth yields and maximal growth rates of mutants impaired in electron transfer or adenosine triphosphatase (uncB). In mutants deficient in menaquinone, cytochromes, or fumarate reductase, these values are considerably lower than in mutants deficient in ubiquinone or a functional adenosine triphosphatase. Electron transfer in this fumarate reductase system leads to the generation of a membrane potential, as is indicated by the uptake of the lipophilic cation triphenylmethylphosphonium by membrane vesicles prepared from cytochrome-sufficient and uncB cells. The generation of a proton-motive force by the fumarate reductase system was also demonstrated by the uptake of amino acids under anaerobic conditions in membrane vesicles of cytochrome containing and uncB cells grown under glycolytic conditions. Membrane vesicles of cytochrome-deficient cells failed to accumulate triphenyl-methylphosphonium and amino acids under these conditions, indicating that cytochromes are essential for the generation of a proton-motive force. Using glutamine uptake as an indication of the generation of ATP and proline uptake as an indication of the generation of a proton-motive force, it was demonstrated in whole cells that the proton-motive force is formed by ATP hydrolysis in cytochrome-deficient cells and by electron transfer in the uncB cells. In cytochrome-containing cells it was not possible to distinguish between these two possibilities, but the growth parameters suggest that, under glycolytic conditions, the proton-motive force is generated via electron transfer in the fumarate reductase system rather than via ATP hydrolysis.
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PMID:Energy supply for active transport in anaerobically grown Escherichia coli. 36 96

In the present work the uptake of foreign materials by macrophages has been studied in order to elucidate its possible energy-dependent mechanisms. We used monolayer cultures of macrophages from human peripheral venous blood, treated with the following metabolic inhibitors: iodoacetic acid, fluoroacetic acid, sodium fluoride, sodium malonate, sodium azide, 2-4-dinitrophenol, cycloheximide, and ouabain. The test assay was performed by using a zymosan particles suspension in Mc Coy 5 A medium supplemented as follows. The quantitation of phagocytosis was obtained by direct count of intracellular zymosan particles by oil 100X microscopy and the results were submitted to a statistical evaluation. The most effective inhibitor we found was iodoacetate, an inhibitor of anaerobic glycolysis, but fluoride, which acts on the same metabolic pathway at a different site, was quite ineffective. The same ineffectiveness we found for fluoracetate and malonate which act on the Krebs cycle. On the contrary, dinitrophenol (uncoupler of oxidative phosphorylation), azide (inhibitor of cytochrome linked-phosphorylation), ouabain (inhibitor of membrane ATPase activity) and cycloheximide (inhibitor of protein synthesis) give a remarkable decrease of index of phagocytosis after a 3h incubation. In conclusion, we can suppose that the energy-dependent phagocytosis is first depending on transport across the cell membrane (ATPase activity and protein synthesis) and second both on anaerobic glycolysis and oxidative phosphorylation.
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PMID:The influence of some metabolic inhibitors on in vitro phagocytizing macrophages. I. The behaviour of human macrophages. 91 75

Anaerobiosis, various respiratory inhibitors and certain agents altering cellular energetics profoundly affect the staphylocidal action of the cationic proteins from rabbit polymorphonuclear leucocytes. It is suggested that sensitivity to these proteins depends on the structure of the cell membrane as influenced by (1) the oxidation level of the cytochrome chain and (2) its energized state. Agents such as amytal and rotenone, which cause a block at the beginning of the chain and would increase its oxidation level, enhance killing, whereas those causing a block in or at the end of the chain, such a 2-n-heptyl-4-hydroxyquinoline-N-oxide, cyanide and anaerobiosis, which would cause reduction of a part or whole of the chain, prevent killing. Among agents altering the energized state of the membrane, dicyclohexyl-carbodi-imide, an ATPase inhibitor, does not prevent killing, whereas 2,4-dinitrophenol, carbonylcyanide-trifluoromethoxy-phenylhydrazone and 5-Cl, 3-t-butyl, 2'-Cl, 4'-NO2-salicylanilide, all uncouplers and ionophores for a specific ion, do prevent killing, although gramicidin, a relatively nonspecific ionophore, does not. The paper also contains an extension of previous work on the effect of iron and haematin, to include various other iron compounds and haematin derivatives.
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PMID:Factors affecting the susceptibility of staphylococci to killing by the cationic proteins from rabbit polymorphonuclear leucocytes: the effects of alteration of cellular energetics and of various iron compounds. 99 90

In the preceding paper the preparation and characterization of antiserum to purified D-lactate are described. In this paper the effects of the antibody on D-lactate dehydrogenase activity and D-lactate-dependent active transport in native Escherichia coli ML 308-225 membrane vesicles and ML 308-225dld-3 vesicles reconstituted with D-lactate dehydrogenase are described. The results demonstrate that D-lactate dehydrogenase is inaccessible to antibody in native ML 308-225 vesicles, but readily accessible to antibody in reconstituted dld-3 vesicles. The findings indicate that D-lactate dehydrogenase is located on the inner surface of native ML 308-225 vesicles and on the outer surface of reconstituted dld-3 vesicles. The results with the native vesicle preparations also provide further evidence that virtually none of the vesicles is inverted or sufficiently damaged to allow access of antibody to D-lactate dehydrogenase. In addition, experiments are presented which demonstrate that an impermeable electron carrier, reduced 5-N-methylphenazonium-3-sulfonate, drives active transport in native ML 308-225 vesicles as well as its permeable analogue reduced phenazine methosulfate. Thus, reduction of the respiratory chain from either side of the vesicle membrane is able to drive active transport. Ca2+, Mg2+-stimulated ATPase is also inaccessible to antibody in ML 308-225 vesicles unless the preparation is subjected to ultrasonic sound, incubated in Tris buffer at pH 9.0, or homogenized vigorously. Moreover, as opposed to D-lactate dehydrogenase and cytochrome b1, ATPase is readily lost from the membrane during the preparation of vesicles.
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PMID:Localization of D-lactate dehydrogenase in native and reconstituted Escherichia coli membrane vesicles. 109 88


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