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Query: EC:3.6.3.1 (Mg2+-ATPase)
 1,484 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of ATPase was studied in highly purified rat liver and thymus cell nuclei, HCO3-, CO3(2-) and SO3(2-) stimulated nuclear ATPase in 1.5--2 times. HSO3- did not affect the enzyme activity, and NO3-, J-, ClO4-,F- and SCN- inhibited it. Bicarbonate increased V and decreased Ka for ATP. SCN- inhibited HCO3--ATPase activity non-competitively with respect to HCO3-. Mg2+-ATPase activity did not depend on pH, and HCO3-component of the activity was decreased under alkaline pH. Mg2+, Mn2+ and Co2+ increased the initial ATPase activity and helped its stimulation with HCO3-. Ba2+, Ni2+ and Zn2+ inhibited the ATPase activity, and Ca2+ did not affect it, Nuclear ATPase is sensitive to 2,4-dinitrophenol and DNAase. It is suggested that cell nuclei have their own H+-ATPase differing for some characteristics from mitochondrial H+-ATPase.
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PMID:[Investigation of adenosinetriphosphatase activity of rat liver and thymus cell nuclei]. 3 23

1. The transduction of energy from the oxidation of substrates by the electron transport chain or from the hydrolysis of ATP by the Mg2+-ATPase was measured in everted membrane vesicles of Escherichia coli using the energy-dependent quenching of quinacrine fluorescence and the active transport of calcium. 2. Treatment of everted membranes derived from a wild-type strain with the chaotropic agents guanidine-HC1 and urea caused a loss of energy-linked functions and an increase in the permeability of the membrane to protons, as measured by the loss of respiratory-linked proton uptake. 3. The coupling of energy to the quenching of quinacrine fluorescence and calcium transport could be restored by treatment of the membranes with N,N'-dicyclohyexylcarbodiimide. 4. Chaotrope-treated membranes were found to lack Mg2+-ATPase activity. Binding of crude soluble Mg2+-ATPase to treated membranes restored energy-linked functions. 5. Membranes prepared from a wild-type strain grown under anaerobic conditions in the presence of nitrate retained respiration-linked quenching of quinacrine fluorescence and active transport of calcium after treatment with chaotropic agents. 6. Everted membrane vesicles prepared from an Mg2+-ATPase deficient strain lacked respiratory-driven functions when the cells were grown aerobically but were not distinguishable from membranes of the wild-type when both were grown under anaerobic conditions in the presence of nitrate. 7. It is concluded (a) that chaotropic agents solubilize a portion of the Mg2+-ATPase, causing an increase in the permeability of the membrane to protons and (b) that growth under anaerobic conditions in the presence of nitrate prevents the increase in proton permeability caused by genetic or chemical removal of the catalytic portion of the Mg2+-ATPase.
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PMID:Energy transduction in Escherichia coli. The effect of chaotropic agents on energy coupling in everted membrane vesicles from aerobic and anaerobic cultures. 13 39

Anion dependence of (Ca2+ + K+)-stimulated Mg2+-dependent transport ATPase and its phosphorylated intermediate have been characterized in both "intact" and "broken" vesicles from endoplasmic reticulum of rat pancreatic acinar cells using adenosine 5'-[gamma-32P] triphosphate ([gamma-32P]ATP). In intact vesicles (Ca2+ + K+)-Mg2+-ATPase activity was higher in the presence of Cl- or Br- as compared to NO3-, SCN-, cyclamate-, SO4(2-) or SO3(2-). Incorporation of 32P from [gamma-32P]ATP into the 100-kDa intermediate of this Ca2+ATPase was also higher in the presence of Cl-, Br-, NO3- or SCN- as compared to cyclamate-, SO4(2-) or SO3(2-). When the membrane permeability barrier to anions was abolished by breaking vesicle membrane with the detergent Triton X-100 (0.015%) (Ca2+ + K+)-Mg2+ATPase activity in the presence of weakly permeant anions, such as SO4(2-) and cyclamate-, increased to the level obtained with Cl-. However, 32P incorporation into 100-kDa protein was still higher in the presence of Cl- as compared to cyclamate-, indicating a direct effect of Cl- on the Ca2+ATPase molecule. The anion transport blocker 4,4-diisothiocyanostilbene-2,2-disulfonate (DIDS) inhibited (Ca2+ + K+)-Mg2+ATPase activity to about 10% of the Cl- stimulation level, irrespective of the sort of anions present in both intact and broken vesicles. This indicates a direct effect of DIDS on (Ca2+ + K+)-Mg2+ATPase. K+ ionophore valinomycin influenced (Ca2+ + K+)-Mg2+ATPase activity according to the actual K+ gradient: Ko+ greater than Ki+ caused inhibition, Ko+ less than Ki+ caused stimulation. From these results we conclude that Ca2+ transport into endoplasmic reticulum is coupled to ion movements which must occur to maintain electroneutrality.
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PMID:Anion dependence of Ca2+ transport and (Ca2+ + K+)-stimulated Mg2+-dependent transport ATPase in rat pancreatic endoplasmic reticulum. 295 52

Ethacrynic acid (EA) highly sensitive Mg2+-ATPase activity was demonstrated in rat brain microsomes. Marker enzyme studies suggested that the EA highly sensitive Mg2+-ATPase activity originated mainly from plasma membranes, and possibly from synaptic vesicles. Oligomycin did not affect the EA highly sensitive Mg2+-ATPase activity. Sulfhydryl reagents, such as N-ethylmaleimide and 5,5'-dithiobis-(2-nitrobenzoic acid), and anion transport inhibitors, such as 4-acetamide-4'-isothiocyanostilbene-2,2'-disulfonic acid, 4,4'-diisothiocyano-stilbene-2,2'-disulfonic acid and 2,4-dinitro-1-fluorobenzene, completely inhibited the EA highly sensitive Mg2+-ATPase activity with apparent Ki values at 5, 5, 8, 8 and 10 microM respectively. Treatment of microsomes with ethylenediaminetetraacetic acid and ammonium sulfate increased the EA highly sensitive Mg2+ and Na+,K+-ATPase activities, but not EA less sensitive Mg2+- or HCO3-ATPase activity, 2- to 3-fold that in crude microsomes. Relative substrate specificities of ATP much greater than GTP greater than ITP greater than UTP, CTP, a Km for ATP at 0.77 mM, and an optimal pH at pH 7.4 were observed. Among the anions tested (Cl-, Br-, F-, HCO3-, I-, SCN-, NO3-), EA highly sensitive Mg2+-ATPase activity was stimulated significantly by Cl- and reduced by NO3-. These data suggest that a novel, plasma membrane-located and anion-sensitive Mg2+-ATPase activity exists in the brain.
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PMID:Novel microsomal anion-sensitive Mg2+-ATPase activity in rat brain. 298 56

We have identified an anion-sensitive Mg2+-ATPase in adenohypophyseal secretory granule membranes. This enzyme is unaffected by sodium, ouabain, and calcium. By electron microscopic morphology, sedimentation properties, nucleotide substrate utilization, and marker enzyme studies, this activity is clearly shown to be intrinsic to the granule membranes. The kinetics for ATP saturation were complex, as curvilinear Lineweaver-Burk plots were obtained with 2 mM magnesium. However, an approach to linearity was obtained (Km for ATP, approximately 0.27 mM) with low concentrations of free magnesium. Many anions and anion-transport blockers significantly influenced enzyme activity. Stimulatory anions in decreasing order of potency were bisulfite greater than sulfite greater than isethionate greater than bicarbonate; Ka values were 2.5 mM for sulfite and 10.8 mM for bicarbonate. Acetate, borate, chloride, citrate, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid, 2-(N-morpholino)ethanesulfonic acid, nitrite, oxalate, 1,3-piperazinediethanesulfonic acid, and sulfate were without major effect. Inhibitory anions in decreasing potency order were azide greater than thiocyanate greater than fluoride greater than nitrate. Anionic stimulation of the granule membrane Mg2+-ATPase linearized the Lineweaver-Burk plots by shifting the enzyme to its higher Km state. In addition, sulfite competitively reversed the produce inhibition exerted by ADP. Anion transport-blockers inhibited the enzyme; of those tested, the most potent was 4-acetamido-4-isothiocyano-stilbene-2,2'-disulfonic acid, with a Ki of 0.17 mM; pyridoxal phosphate, sulfisoxazole, and ethacrynic acid also inhibited enzyme activity. The protein-binding dye p-sulfobenzene-azo-o-sulfobenzene-azo-beta-naphthol-3,6-disulfonic acid, structurally similar to transport blockers, was a potent inhibitor, with a Ki of 2.8 mM. These data on pituitary secretory granule ATPase raise the possibility that the granule membranes may function in anion or proton transport, perhaps in relation to exocytosis and hormone secretion.
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PMID:Identification and characterization of an anion-sensitive Mg2+-ATPase in pituitary secretory granule membranes. 611 65

Rat blood was incubated at 37 degrees C for 60 min with either NaNO3 or NaNO2 to examine the relationship between the decrease in the hexose content and Ca2+,Mg2+-ATPase activity of red cell membranes, and NO3- and NO2-. The hexose content decreased depending on the NaNO2 concentration up to 100 microM reaching 76% (p less than 0.05) of the control value. NaNO3 had little effect on the hexose content. On the other hand, the Ca2+,Mg2+-ATPase activity decreased depending on the NaNO3 concentration up to 200 microM, where the activity reached 75% (p less than 0.01) of the control value. The effect of NaNO2 on this activity was smaller than that of NaNO3. The sialic acid content and the Na+,K+-ATPase activity did not show significant alterations by incubation with NaNO2 and NaNO3 at below 100 microM. To examine the in vivo effects of NO2- and NO3-, 50 mM NaNO3 was intravenously injected into rats five times at hourly intervals (dose: 1.0 ml/kg body weight), and blood was collected 1 hr after the last injection. The activities of Ca2+,Mg2+- and Na+,K+-ATPases of red cell membranes were decreased to 68% (p less than 0.05) and 80% of the control value, respectively. Reduction by injection of 50 mM NaNO2 was smaller than that by 50 mM NaNO3. The results show that the hexose content and the Ca2+,Mg2+-ATPase activity of red cell membranes were decreased by NO-x that increased in the blood during short-term exposure of rats to NO2.
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PMID:Effects of nitrate and nitrite, chemical intermediates of inhaled nitrogen dioxide, on membrane components of red blood cells of rats. 614 34

Gentamicin and neomycin-resistant mutants of Escherichia coli K-12 were isolated some of which were resistant to nitrofurans, chlorate, P1 and lambda bacteriophages as well as to all aminoglycoside antibiotics tested. Previously isolated nitrofuran-resistant mutants were not cross-resistant to the tested aminoglycosides, chlorate and bacteriophages. The aminoglycoside-resistant mutants exhibiting cross-resistance had enhanced membrane Mg2+-ATPase and decreased periplasmic alkaline phosphatase activity compared to their parent sensitive strains. The mutants were also defective in the fermentation of sugars, reduction of nitrate and nitrite, and in formate dehydrogenase activity. Preliminary genetic studies indicated that the pleiotropic mutation might be located in the upper left quadrant of the E. coli K-12 chromosome linkage map. It is postulated that such mutants with gross membrane alterations have impaired accumulation of aminoglycoside and nitrofuran antibiotics.
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PMID:Gentamicin- and neomycin-resistant mutants of Escherichia coli K-12 cross-resistant to nitrofurans. 614 38

Highly purified tonoplast and plasma membrane vesicles were isolated from microsomes of Arabidopsis thaliana by preparative free-flow electrophoresis. The most electronegative fractions were identified as tonoplast using nitrate-inhibited Mg2+-ATPase as enzyme marker. The least electronegative fractions were identified as plasma membrane using glucan-synthase II, UDPG: sterol-glucosyl-transferase, and vanadate-inhibited Mg2+-ATPase as enzyme markers. Other membrane markers, latent inosine-5'-diphosphatase (Golgi), NADPH-cytochrome-c reductase (endoplasmic reticulum) and cytochrome-c oxidase (mitochondria) were recovered in the fractions intermediate between tonoplast and plasma membrane. Immunoblot analysis of membrane fractions by antibodies directed against tonoplast and plasma membrane proteins confirmed the nature and the purity of the isolated membranes. The cytoskeletal protein actin, which was also identified by immunoblotting, was found to be specifically attached to the plasma membrane vesicles. The structural and functional integrity of the isolated membranes from Arabidopsis thaliana is discussed in the light of results obtained for the location of receptors and enzymes, or for the determination of ligand binding activity.
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PMID:Free-flow electrophoresis for fractionation of Arabidopsis thaliana membranes. 966 77

By the method of hydroponic culture, this paper studied the alleviation effects of LaCl3 on the photosynthetic characteristics of cucumber seedlings under nitrate (140 mmol NO3(-) x L(-1)) stress, with the related mechanisms discussed. Under nitrate stress, the seedlings leaf chlorophyll and carotenoids contents decreased significantly, and the leaf Mg2+-ATPase, Ca2+-ATPase activities also decreased. On the 7th day of nitrate stress, the decrease of seedlings photosynthetic rate was mainly due to stomatal limitation; but on the 12th day of nitrate stress, the decrease was mainly due to no-stomatal limitation. Supplement with LaCl3 could make the cucumber seedlings keep relatively higher leaf Mg2+-ATPase and Ca2+-ATPase activities and chlorophyll and carotenoids contents, and applying 20 micromol x L(-1) of LaCl3 could increase the carotenoids content significantly. LaCl3 could also improve the leaf gas exchange, and alleviate the decrease of leaf Fv/Fm, PhiPSII, AQY, CE, and qp under nitrate stress, which helped the leaves making good use of light energy and maintaining higher CO2 assimilation capacity. An additional 20 micromol x L(-1) of LaCl3 could alleviate the nitrate stress on the photosynthesis of cucumber seedlings efficiently, but an additional 200 micromol x L(-1) of LaCl3 only had the alleviation effect at the initial period of nitrate stress. Our results could benefit to the improvement of greenhouse soil.
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PMID:[Alleviation effects of LaCl3 on photosynthetic characteristics of cucumber seedlings under nitrate stress]. 2013 1