Gene/Protein Disease Symptom Drug Enzyme Compound
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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)

Properties of HCO--3-stimulated ATPase from rat heart muscle nuclei were studied. The maximal activity of HCO--3-ATPase was observed at concentration of bicarbonate 25 mM. The enzyme had a pH optimum at pH 8.0-8.5. Bicarbonate stimulated the ATPase activity only in presence of Mg2+, Mn2+ and Zn2+, Co2+, Cd2+ and Ca2+ were ineffective. NaCO3 and Na2SO3 at concentration 30 mM stimulated the nuclear ATPase activity by 20% and 81%, respectively. Anions N3--, scn--, clO--4, and I-- inhibited both Mg2+-ATPase and HCO--3-ATPase. HSO--3 and SO2--4 ions did not affect the nuclear ATPase activity.
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PMID:[Anion-sensitive nuclear ATPase of the rat heart]. 2 54

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

Activity of ATPases was studied in erythrocytes of patients with phobia neurosis of the 11 degree and in erythrocytes of mentally healthy patients. The total Mg2+, Na+, K+-dependent ATPase activity of patients with the neurosis was unaltered in blood. But the Mg2+-ATPase activity was increased and the Na+, K+-ATPase activity was decreased in the patients as compared with the control group. Addition of lithium carbonate into incubation mixtures exhibited different effect on the Na+, K+-stimulated ATPase depending upon the initial activity of the enzyme. In blood of patients with low initial values of the enzymatic activity it was increased. But the Na+, K+-ATPase activity was decreased by lithium carbonate in those cases when the initial enzymatic activity was high. Quantitatively the effect of lithium on the enzymatic activity was similar in the both groups of neurotic patients studied (although the direction of changes was oposite).
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PMID:[Activity of Mg 2+, Na+ and K+ stimulated ATPase in erythrocytes of patients with phobic neurosis and the effect of lithium carbonate on the enzymatic activity]. 12 54

In homogenate and mitochondria of cortex and medulla of rat kidney a stimulating effect of different concentrations of bicarbonate on the ATPase activity was studied. By the rate of inhibition of Mg2+-ATPase and HCO3-ATPase, thiocyanate, perchlorate and azide were distributed as follows: N3 greater than CNS greater than ClO4. Thiocyanate inhibited non-competitively the HCO3-stimulated ATPase activity. The similarity was observed between HCO3-stimulated ATPase from rat kidney and bicarbonate-stimulated ATPase from other cells.
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PMID:[HCO3- -stimulated ATPase of rat kidneys]. 19 92

Isolated choroid plexuses from rabbits were used to determine uptake and accumulation of 10(-5) M radiolabelled choline (expressed as tissue/medium ratio) and the activities of various types of ATPases (based on ouabain inhibition and bicarbonate stimulation) following pre-treatment of the animals with 0.5 mg kg-1 17-beta-oestradiol, alone or in combination with 2 mg kg-1 progesterone. The combined treatment reduced the choline uptake by 35% and also lowered the activity of Na+,K+-ATPase by 31%, without influencing tissue wet weight. The reduction in HCO3-ATPase was smaller and not statistically significant. There was a tendency also for oestrogen alone to lower these activities, but only by less than 20%. The Ca2+,Mg2+-ATPase activity was not significantly affected by any of the hormones.
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PMID:Changes in transport functions of isolated rabbit choroid plexus under the influence of oestrogen and progesterone. 254 64

Bicarbonate-stimulated Mg2+ dependent ATPase activity was demonstrated both biochemically and cytochemically, in brush border membranes from rat, rabbit and guinea pig duodenum. There was no correlation between enzyme activity and basal HCO3- secretion rates in the different species. The concentration of HCO3- necessary for optimal stimulation of ATPase activity, degree of stimulation and total activity was higher in the rat than in other species. Activity was higher in rat duodenum than in the ileum. This is consistent with the proposed electrogenic HCO3- secretion in the duodenum. Distribution of activities of alkaline phosphatase and HCO3(-)-stimulated Mg2+-ATPase along the duodenal villus showed significant differences, suggesting that the two activities reflect, at least in part, distinct enzymes.
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PMID:Biochemical and cytochemical comparison of intestinal bicarbonate-stimulated Mg2+ dependent ATPase and alkaline phosphatase activities in rat, rabbit and guinea pig. 295 98

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

Studies were performed to characterize ethacrynic acid (EA) highly sensitive Mg2+-ATPase isolated from microsomal fractions of the rat brain. The functional molecular sizes of the EA highly sensitive and EA less sensitive Mg2+-ATPases, estimated by a radiation inactivation method, were 480 and 80 kDa, respectively. An anion transport inhibitor, 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid (SITS) inhibited the EA highly sensitive Mg2+-ATPase activity. The type of inhibition was uncompetitive with respect to ATP, and the inhibition was suppressed by anions such as Cl-, Br- and I-. Chloride ions stimulated enzyme activity with an increase in Vmax, but not in Km, for ATP. Anions tested also increased the enzyme activity in the following order of decreasing potency: Cl- greater than Br- greater than CH3COO- = I- greater than SO4(2-) = HCO3- greater than SO3(2-). These results suggest that EA highly sensitive Mg2+-ATPase is a relatively large molecule with anion-sensitive sites that affect the ATP hydrolyzing activity and the SITS binding capacity through anions, with Cl- being the most potent.
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PMID:Characteristics of ethacrynic acid highly sensitive Mg2+-ATPase in microsomal fractions of the rat brain: functional molecular size, inhibition by SITS and stimulation by Cl-. 302 85

Basal-lateral and brush border membranes from pig kidney cortex were prepared by differential centrifugation followed by free-flow electrophoresis. In each type of membrane, azide-insensitive, low-affinity Ca2+-ATPase and Mg2+-ATPase activities are demonstrated. A comparative study for both membranes further reveals the following analogies between these ATPases: (a) they show maximal activity between pH 8 and 8.5; (b) they exhibit Km values for Ca-ATP or Mg-ATP in the millimolar range and have a comparable low substrate specificity; (c) they are insensitive to 10 microM of vanadate, N,N'-dicyclohexylcarbodiimide, e diethylstilbestrol, quercetin, harmaline and amiloride. The partial inhibition by 1 mM of the various compounds is rather aspecific. In view of these similarities it is concluded that only one enzyme entity is responsible for the activity which is measured in both membrane types. The HCO3-stimulated Mg2+-ATPase activity in pig kidney cortex was also studied. This enzyme, however, is clearly of mitochondrial origin since the HCO3-stimulation coincides with the distribution profile of succinate dehydrogenase, a mitochondrial marker; and since it is inhibited by azide.
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PMID:An azide-insensitive low-affinity ATPase stimulated by Ca2+ or Mg2+ in basal-lateral and brush border membranes of kidney cortex. 316 26

Na+,K+-ATPase, HCO3(-)-ATPase, Ca2+,Mg2+,-ATPase, Ca2+-ATPase, and alkaline phosphatase activities were measured in cultures of osteoblastlike cells treated with fluoride and cortisol separately and in combinations. Low concentrations of cortisol increased HCO3- -ATPase (10(-11) to 10(-18) M cortisol) and alkaline phosphatase (10(-11) to 10(-9) M cortisol) activities, but higher cortisol concentrations reduced these activities. Na+,K+-ATPase, Ca2+,Mg2+-ATPase, and Ca2+-ATPase activities tended only to be reduced by cortisol. Fluoride (10(-6) and 5 X 10(-6) M) increased HCO3(-)-ATPase and alkaline phosphatase activities, but these activities were similar to controls in the presence of 10(-5) M fluoride. Ca2+,Mg2+-ATPase activity was decreased and Na+,K+-ATPase activity was increased as the concentration of fluoride increased (10(-6) to 10(-5) M). Preliminary experiments with fluoride indicated that lower concentrations (10(-7) M) were without effect. Cortisol concentrations of 10(-9) and 10(-8) M were chosen for studies with combinations of cortisol and fluoride because the effects of these concentrations on alkaline phosphatase activity were opposite, i.e. 10(-9) M increased whereas 10(-8) M decreased activity. Fluoride concentrations of 10(-6), 5 X 10(-6), and 10(-5) M were chosen because a peak of alkaline phosphatase activity occurred at 5 X 10(-6) M fluoride. Higher (10(-4) M) and lower (10(-7) M) fluoride concentrations were without effect. The effects of combinations of cortisol and fluoride depend on the enzyme activity measured. Fluoride (10(-6) M) combined with cortisol (10(-9) M) produced a peak of Na+,K+-ATPase activity. The increased activity obtained with all concentrations of fluoride alone was preserved when fluoride was combined with 10(-8) M cortisol, although the activity tended to be reduced at 5 X 10(-6) and 10(-5) M fluoride. HCO3(-)-ATPase activity was increased by fluoride combined with 10(-8) M cortisol and decreased by fluoride combined with 10(-9) M cortisol compared to the activities obtained with fluoride alone. The decrease in Ca2+,Mg2+-ATPase activity caused by fluoride alone was prevented by 10(-9) and enhanced by 10(-8) M cortisol, although all treatments produced the same activity at 10(-5) M fluoride. Ca2+-ATPase activity tended to be increased by combinations of fluoride and cortisol, but significantly so only at 10(-5) M fluoride in combinations with 10(-8) and 10(-9) M cortisol.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Effects of cortisol and fluoride on ion-transporting ATPase activities in cultured osteoblastlike cells. 609 29


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