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)

Phosphorylating submitochondrial particles from beef heart (ETPH) prepared here contained about 2.4 nmol of ATP and 1.9 nmol of ADP/mg of protein after repeated washing of the particles. Essentially all of the "tightly bound " ATP and ADP was removed by trypsin treatment. The trypsin-treated ETPH had increased ATPase activity, undiminished NADH oxidase and succinate oxidase activity, but energy-coupling activity (ATP-driven reversed electron transfer) was abolished. Removal of half the ATP and ADP occurred at low levels of trypsin and was associated with loss of half of the coupling activity. Gel filtration of ETPH in high ionic strength buffer also removed ADP and ATP from the particles, resulting in loss of energy-coupling activity, while ATPase activity was increased. The results support the contention that the tightly bound ADP is essential in energy coupling in mitochondria. Tightly bound ATP may also play an essential role.
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PMID:Removal of "tightly bound" nucleotides from phosphorylating submitochondrial particles. 13 46

An electrophilous inhibitor, p-(N,N-di-2-chloroethyl)amino-phenylacetic acid (I), specifically disturbs the mechanism of respiration and phosphorylation coupling in mitochondria. I inhibits respiration and ATPase activity in intact mitochondria and does not affect these processes in mitochondria and submitochondrial particles with partially or completely impaired coupling system. The data obtained show that I inhibits protonophoric function of NADH-ferricianide reductase from submitochondrial particles soluble ATPases from bovine heart and Micrococcus lysodeikticus mitochondria adsorded on octane water interface and has no effect on respective enzymes in water solutions. Cation-transferring enzymes are shown to behave with respect to the inhibitor on lipid water interface like respective enzymes in intact mitochondria, while in water solutions they behave like those in systems with the impaired coupling mechanism. Effect of I on protonophoric function of oligomycin-sensitive ATPase and bacteriorhodopsin plaques isolated from Halobacterium halobium is also studied. It is shown that the precence or the absence of I effect is due to a nature of lipid in the enzymatic complex. I is found also to inhibit specifically the transport of Ca2+ from water to octane in the presence of Ca2+-ATP-ase from rabbit sarcoplasmic reticulum.
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PMID:[Mechanism of action of the specific inhibitor of respiration and phosphorylation in mitochondria--n-(N,N-di-2-chlorethyl)aminophenylacetic acid]. 13 99

The mechanism of action of some quinoline alkaloids and their derivatives on respiratory chain of rat liver and Candida lipolytica yeast mitochondria was studied. The alkaloids were shown to inhibit electron transfer in the respiratory chain. The site of their action is localized between b and c cytochromes. Besides their ability to inhibit electron transfer in the respiratory chain, alkaloids are shown to be specific inhibitors of "exogenous" NADH-dehydrogenase of C. lipolytica yeast mitochondria. In addition to their inhibiting properties alkaloids can stimulate ATPase activity of mitochondria. O-alkylation of pseudane-IX permits to differentiate the inhibiting and uncoupling properties of this alkaloid.
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PMID:[Mechanism of action of some quinoline alkaloids on respiratory chain of mitochondria]. 13 72

The masseter muscles of different mammals were studied by means of hisotchemical reactions: NADH: Nitro BT oxidoreductase (NADHOX), 3-hydroxybutyrate: NAD+ oxidoreductase (HBOX), glycerol-3-phosphate: menadione oxidoreductase (GPOX), and acid-stable and alkali-stable myosin adenosine triphosphatase (ATPase). The masseter mucles of cattle and sheep consisted only of the fibres that reacted moderately for GPOX and strongly for NADHOX, HBOX, and the acid-stable ATPase. The masseter fibres of rats and guinea pigs reacted uniformly and strongly for GPOX and the alkali-stable ATPase. The fibres of the rats showed a weak to strong reaction for NADHOX and mostly a negative reaction for HBOX, whereas those of the guinea pigs reacted uniformly and strongly for NADHOX and HBOX.The masseter fibres of swine and dogs showed a weak or strong reaction for the alkali-stable and a negative or weak reation for HBOX. The fibres of the swine were weak to strong in NADHOX activity and those of the dogs uniformly strong; the fibres of the two species gave a moderate to strong reaction for GPOX. The masseter fibres of the ruminant differed from those of the other species in histochemical properties, and appeared to have the histochemical characteristics that meed functional demands for slow, long-term exercise.
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PMID:A comparative histochemical study of the masseter muscle of the cattle, sheep, swine, dog, guinea pig, and rat. 13 87

Human adult lung fragments removed from macroscopically undamaged and anthracosis exempted zones of lungs of 20 pneumonectomies made for cancer, were tested for 25 enzymic activities. The location and intensities of these enzymic activities were different in the lung tissue components; The bronchial epithelia contained highly active LDH, MDH, SDH, NADH-TR and NADPH-TR, glucose-6-phosphate dehydrogenase, active hydroxyproline-2-epimerase, alkaline phosphatase. Ca2+-activated ATP-ase, and beta-galactosidase. Bronchial and vascular muscles presented intense activities of LDH, MDH and SDH of alkalinephosphatase, AMP-ase and Ca2+-activated ATP-ase, as well as of beta-galactosidase. The alveolar walls presented high activities of SDH, MDH and LDH, of alkaline and acid phosphatases, of beta-galactosidase and of Tween-40 and 60-esterases, of HEP, cytochrome-oxidase and peroxidase. The free alveolar macrophages were active for LDH, MDH, SDH, NADH-TR and NADPH-TR, G1-6-ph-DH, acid and alkaline phosphatase, cytochrome-oxidase and peroxidase, HEP, AMP-ase and Mg2+-activated ATP-ase, Tween-esterases, naphthol-ASD-acetate esterase, and beta-galactosidase. The endothelia contained high activities of alkaline phosphatase, of AMP-ase and Mg2+-activated ATPase, of LDH, MDH and SDH, and of beta-galactosidase. In bronchial lymphoid nodules it was the LDH, MDH, SDH, cytochrome-oxidase and peroxidase, HEP, alkaline phosphatase and AMP-ase, Tween-60-esterase and beta-galactosidase that were active. The interlobular areas of the lung presented intense activities of SDH, MDH, LDH, HEP and cytochrome-oxidase. The activities of the other tested enzymes were weaker or absent in the adult human lung components, the same as those of aminopeptidases which were present only in some free alveolar macrophages. The discussion of some relationships between these enzymic actitivies and the morphology of the human adult lung tissue asserted that the latter could not be considered as a "normal" tissue but as one overstrained by the components of blood and polluted air.
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PMID:Histoenzymology of the lung. I. Enzyme activities of the lung tissue of acult humans; relationships between structure and functions. 14 Mar 14

Enzyme activity of adenosinetriphosphatase, NADH2-tetrazolium reductase and lactate dehydrogenase was studied in the rat perineurium 10, 20, 30, and 90 days post partum. The effect of under-nutrition was shown by a lack of enzyme activity in rats 30 days post partum in contrast to control animals, 30 days also corresponds to the time when, in normal rats, the perineurial diffusion barrier to exogenous macromolecules becomes established. In undernourished rats this diffusion barrier does not appear. At 90 days post partum raised enzyme activities indicate a high metabolic turnover in the perineurium even in animals with undernutrition.
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PMID:Impaired development of the rat perineurium by undernutrition. An enzyme histochemical study. 14 May 82

The histochemistry of the neural cells was studied in the submandibular ganglia of 5 Callithrix jacchus (3 males and 2 females) and 4 Callithrix penicillata (2 males and 2 females). These cells contain neutral mucopolysaccharides, nucleoproteins and lipidic materia, but are apparently devoid of glycogen. It is impossible to demonstrate in them any reactivity for UDPG-GT, phosphorylases, ATPase at pH 6.3, leucine aminopeptidase and alanyl aminopeptidas. The reaction for the other searched enzymes was as follows: weak (F-1,6-P Ald and cytochrome oxidase), weak to moderate (ADH, 6-P-GDH, ICDH, SDH, MDH, alpha-GPDH and beta-OHBDH), moderate (G-6-PDH, F-1,6-PA, LDH and GDH), moderate to strong (ATPase at pH 7.4, nonspecific esterase and acid phosphatase) and strong (G-6-PA, NADH2,-TR, NADPH2-TR, ATPase at pH 8.5 and 9.4 and alkaline phosphatase).
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PMID:Histochemical studies on the submandibular ganglia of marmosets (Callithrix jacchus and Callithrix penecillata). 14 13

The effects of the inhibitors dicyclohexyl-carbodiimide (DCCD), bathophenanthroline and tertiary octylcatechol, on some enzyme activities in membranes from strains of Escherichia coli carrying mutations in the uncB or uncC genes have been studied. Membranes prepared from uncC mutants retain a normal DCCD-sensitive Mg2+-stimulated adenosine triphosphatase (Mg-ATPase) activity whereas in uncB mutants this enzyme activity is insensitive to DCCD. The membrane-bound Mg-ATPase activity from the uncC mutant strain, as compared with that from the normal strain, is only partially sensitive to the inhibitors bathophenanthroline or tertiary-octylcatechol. Both of these inhibitors stimulate the membrane-bound Mg-ATPase from uncB mutant strains. A DCCD-insensitive Mg-ATPase activity is found in the cytoplasmic fraction following cell disruption of either the uncB or the uncC mutants. The lipophilic chelators bathophenanthroline and tertiary-octylcatechol stimulate the activity of the 'soluble' Mg-ATPase in the uncB mutant but partially inhibit the activity in the uncC mutant. The NADH oxidase activities in membranes from both mutant and normal strains are strongly inhibited by tertiary-octylcatechol and bathophenanthroline but not by DCCD.
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PMID:Different effects of inhibitors on two mutants of Escherichia coli K12 affected in the Fo portion of the adenosine triphosphatase complex. 14 61

the toxic effects of CH3HgCL on mitochondria of mammalian organs including human and rat liver were examined. [203Hg]CH3HGCl was bound mainly to mitochondrial proteins. The binding was not effected by the energy state of mitochondria. The state 3 respiration, oxidative phosphorylation and 32Pi-ATP exchange reaction were inhibited by 10 to 50 nmol of CH3HgCl per mg of mitochondrial protein, while NADH-and succinate-dehydrogenase and ATPase were more resistant to it The difference spectrum of the treated mitochondria indicated that the point of inhibition was located after flavin and before cytochrome b. Mitochondrial swelling was induced by CH3HgCl, in accordance with previous morphological observations in vivo. The swelling, stimulation of ATPase and energy-dependent H+ extrusion cauded by CH3HgCl were equally dependent on K+. Under these conditions, uptake of K+ by mitochondria was increased and the membrane potential was dissipated. Unlike the case with other organomercuric compounds, transport of phosphate was not inhibited by CH3HgCl. When tested on liposomes, CH3HgCl itself was not lipid-soluble, as some organomercuric compounds are, and was not an uncoupler or a K+-carrier. It was concluded that protein bound CH3HgS-induced K+ uptake into mitochondria and the resulting loss of membrane potential was the major cause of uncoupling, though at higher concentrations, the electron transport system was also inhibited.
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PMID:Effect of methyl mercury on phosphorylation, transport, and oxidation in mammalian mitochondria. 14 24

Serial frozen sections of longissimus dorsi muscles from seven pigs at different live weights (13 to 127 kg) were reacted for ATPase by the calcium method at an alkaline pH and for NADH oxidative activity. One hundred muscle fibres from each animal were identified individually in serial sections and their staining intensity was measured with a microscope photometer at 600 nm. For each section, staining intensity of fibres (% tranmission) was measured and converted to the nearest one-tenth unit of the range from the darkest to the lightest staining fibres. Frequency of occurrence of fibre types was plotted on a 10 X 10 grid using the range co-ordinates for NADH oxidative activity (vertical) and ATPase activity (horizontal). The commonly recognized histochemical fibre types in this muscle appeared as crowded areas in the grid but, in many cases, these areas were part of a continuous 'L' shaped range, a continuous but skewed distribution with regard to NADH oxidative activity was detected. In fibres with NADH oxidative activity of 0.6 to 1.0 units of the range, a continuous but irregular distribution with regard to ATPase activity was detected. Within this range, there was some evidence of a growth-related shift towards weaker ATPase activity.
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PMID:Transitional stages in the histochemical development of muscle fibres during post-natal growth. 14 16


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