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Query: UMLS:C0847097 (acidity)
 15,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Total phosphorus was estimated after mineralization of a sample, containing organic phosphoesters and proteins; a method is based on the formation of phosphomolybdenovanadium complex at acid pH. The analyses for inorganic phosphorus were carried our together with estimation if some labile phosphoesters (glucose-I-phosphate, ADP, ATP), which was possible due to low acidity of the medium (0.24 N HC1O4), small concentrations of reagents (3.2 mg/ml of molybdate, 0.08 mg/ml vanadate), addition of sodium citrate to neutralize the excess of molybdenovanadium acid and extraction of the colored complex with butyl or isobutyl alcohol. Optical density was measured at two wave lengths (340 nm and 390 nm) which enabled to estimate from 0.5 to 80 microng of phosphrorus in a sample.
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PMID:[Determination of total and inorganic phosphorus in the presence of organic phosphoric acid esters and proteins]. 102 59

Ascorbic acid (AsA), after being oxidized in 0.1 M phosphate (pH 7.0) buffer under the catalytic influence of adventitious iron, reacted with glutamine (Gln) derivatives with the formation of stable fluorophores showing lipofuscin-like blue (350/430 nm) fluorescence. The fluorescence was reversibly quenched by acidity and enhanced by alkaline conditions, and the fluorescence intensity was directly proportional to the Gln and AsA concentrations. Addition of H2O2 considerably increased the velocity of the fluorescence formation. Incubation of AsA/Gln in 0.1 M phosphate buffer at pH 5.0 gave a slower fluorophore formation as compared with incubation at pH 7.0. The iron chelators DTPA and desferrioxamine inhibited the fluorophore development by preventing the iron catalyzed AsA oxidation. This was in contrast to the effects of the chelators ADP and EDTA which did not show such preventive activity. The fluorophores produced by the AsA/Gln reaction are thought to be Schiff bases formed secondary to Maillard reactions involving oxidized AsA. Considering that ascorbic and dehydroascorbic acid are active and common reductones, the oxidation-enhanced carbonyl-protein cross-linking is suggested to be an important chemical reaction which may take place during ageing and be involved in lipofuscinogenesis.
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PMID:Lipofuscin-like fluorophores can result from reactions between oxidized ascorbic acid and glutamine. Carbonyl-protein cross-linking may represent a common reaction in oxygen radical and glycosylation-related ageing processes. 156 Jun 82

Several divalent metal ions were used as kinetic probes of the beef heart mitochondrial adenosinetriphosphatase (F1) under a variety of conditions, and the relationship between the properties of the catalytic metal ion and the catalytic activity of the enzyme was examined. Vmax for ATP hydrolysis was largest when metal ions characterized by intermediate values of acidity of coordinated water molecules (pKa) and metal-nucleotide stability constants (Kstab) were present. As temperature increased, the peak of Vmax vs. pKa (or Kstab) shifted to lower initial values of pKa or Kstab. The solvent deuterium isotope effect on Vmax (DV) was normal and largest when the metal ion present during F1-catalyzed ATP hydrolysis was most acidic and the metal nucleotide stability constant was large. When an active site tyrosine on F1 was nitrated, Vmax was most affected when the metal ion present was least acidic and the metal nucleotide stability constant was small. The isotope effect on V/K (DV/K) was normal, small, and apparently independent of the metal ion present. ADP inhibition of F1-catalyzed ATP hydrolysis is competitive, and the Ki is independent of the metal ion present. The degree of Pi inhibition of F1 is dependent on the metal ion present. The inhibition by Pi is competitive at low temperature and becomes noncompetitive as temperature increases. These and previous results support a mechanism whereby a water molecule coordinated to the metal ion of an enzyme-bound gamma-monodentate metal-ATP complex is deprotonated to begin a series of events whereby a beta,gamma-bidentate metal-ATP complex is produced. Upon hydrolysis, the bond between the metal ion and the beta-phosphate of ADP in the Pi-metal-ADP complex is broken before products (ADP and metal-Pi) are released.
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PMID:Dependence of the activity of beef heart mitochondrial adenosinetriphosphatase on the properties of the catalytic metal ion. 288 48

Membranes from Halobacterium saccharovorum contained a cryptic ATPase which required Mg2+ or Mn2+ and was activated by Triton X-100. The optimal pH for ATP hydrolysis was 9-10. ATP or GTP were hydrolyzed at the same rate while ITP, CTP, and UTP were hydrolyzed at about half that rate. The products of ATP hydrolysis were ADP and phosphate. The ATPase required high concentrations (3.5 M) of NaCl for maximum activity. ADP was a competitive inhibitor of the activity, with an apparent Ki of 50 microM. Dicyclohexylcarbodiimide (DCCD) inhibited ATP hydrolysis. The inhibition was marginal at the optimum pH of the enzyme. When the ATPase was preincubated with DCCD at varying pH values, but assayed at the optimal pH for activity, DCCD inhibition was observed to increase with increasing acidity of the preincubation medium. DCCD inhibition was also dependent on time of preincubation, and protein and DCCD concentrations. When preincubated at pH 6.0 for 4 h at a protein:DCCD ratio of 40 (w/w), ATPase activity was inhibited 90%.
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PMID:Dicyclohexylcarbodiimide-sensitive ATPase in Halobacterium saccharovorum. 293 Oct 49

Fatigue--or decrease in force generation--is a reduction of simultaneously attached cross-bridges in the force generating state. Two processes are necessary for the force generation: Firstly Ca++ release from the sarcoplasmic reticulum to the sarcoplasm and the binding of Ca++ by the troponin molecule and secondly the turnover of myosin-actin cross-bridges. These processes require energy in at least three different ATPase reactions and can consequently be inhibited when ATP hydrolysis is decreased, i.e. when ATP content is to low or when the reaction products (ADP, Pi and H+) reach inhibiting levels or when muscle pH has decreased to values inhibiting actomyosin ATPase activity (22). Low pH will also decrease Ca++ release and Ca++ affinity by troponin (23). In isometric contraction the force is well preserved as long as ADP phosphorylation can be provided by both PCr degradation and anaerobic glycolysis. When the PCr store is exhausted the force starts to decline and if muscle activation is maintained the force will continue to decrease along with falling glycolytic rate. ADP phosphorylation rate decreases successively and ATP content falls with an at least transient increase in ADP. The ATP decrease, apart from the minor increase in ADP, is balanced by an equimolar increase in IMP. Lactate accumulation produces an increasing acidity with muscle pH values down to 6.25. Early changes in free ADP content cannot be excluded as reason for the initial decrease in force production followed by more pronounced inhibition of ATPase activity during continued contraction due to both substrate lack and product inhibition together with pH effect on the excitation--contraction mechanism. In dynamic exercise with supramaximum work intensity the relation between fatigue development and metabolism is similar. In prolonged dynamic exercise relying on oxidative metabolism without lactate formation the point of fatigue is reached when the glycogen store is exhausted. Again ADP phosphorylation rate is decreased when the energy substrate is changed from carbohydrate to fat with lower maximum rate of ATP resynthesis.
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PMID:Biochemistry of muscle fatigue. 396 54

The concentration dependence of the chemical shifts of the protons H-2, H-8, H-10, H-11, and H-1' of 1,N6-ethenoadenosine 5'-monophosphate (epsilon-AMP2-) has been measured. The results are consistent with the isodesmic model of indefinite noncooperative stacking; the association constant, K = 2.5 +/- 0.3 M-1, is within experimental error identical to the value determined earlier for AMP2-,K = 2.1 +/- 0.4 M-1. The conditions for the potentiometric pH titrations, used to determine the acidity constants of H2(epsilon-AMP), H2(AMP), and H(UMP)- and the stability constants of the metal ion (M2+) complexes of the corresponding nucleoside 5'-monophosphates (NMP), were chosen so that the ligands were present in the monomeric form. The stabilities of Mg(epsilon-AMP) and Mg(AMP) are similar; however, the stabilities of the Mn2+, Cu2+ and Zn2+ complexes of epsilon-AMP2- are much larger (in the case of Cu2+ by a factor of 700) than those of AMP2-. This is due to the much larger metal ion affinity of the epsilon-adenosine moiety compared to that of the parent adenosine residue. As the uridine moiety does not participate in complex formation, the stability constants of M(UMP) have been used to evaluate the extent of macrochelation (i.e. the simultaneous coordination of M2+ to the base moiety and the phosphate group) in the epsilon-AMP and AMP complexes: the concentration of the macrochelated isomer is considerably larger for M(epsilon-AMP) than for M(AMP). A comparison with previous results for the complexes with ADP3- and ATP4- indicates the order, M(AMP)cl less than M(ADP)-cl greater than M(ATP)2-cl for the tendency to form macrochelates (cl). Due to the relatively high affinity of the epsilon-adenosine moiety towards Mn2+, Cu2+ and Zn2+, the phosphate-monoprotonated complexes M(H . epsilon-AMP)+ also become important; the corresponding complexes play only a minor role in the M2+/AMP systems. Intramolecular aromatic-ring stacking occurs in the ternary Cu(2,2'-bipyridyl)(NMP) complexes: about 80% of Cu(Bpy)(AMP) and Cu(Bpy)(epsilon-AMP) exist as the stacked isomer in aqueous solution; for the former system it has been shown in a previous X-ray study that the intramolecular ligand-ligand interaction occurs also in the solid state [Aoki, K. (1978) J. Am. Chem. Soc. 100, 7106]. Overall, the results emphasize that great care should be exercised in drawing conclusions based on studies of metal-ion-containing enzymic systems in which the natural adenine nucleotide cofactors have been replaced by the corresponding 1,N6-etheno derivatives.
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PMID:On the metal-ion coordinating properties of the 5'-monophosphates of 1, N6-ethenoadenosine (epsilon-AMP), adenosine and uridine. Comparison of the macrochelate formation in the complexes of epsilon-AMP, AMP, ADP and ATP. 632 Nov 71

Effects of 3,3',5'-triiodothyronine (rT3) in connection with 3,3',5-triiodothyronine (T3) on 3T3 cells were studied in vitro by means of 1H and 31P NMR spectroscopy. In the cells incubated with 5 nM T3 for 3 h at pH 7.4, the ATP/ADP ratio was elevated from 6.9 to 8.4, whereas it was reduced to 6.1 in cells incubated with rT3. When the cells were incubated at pH 6.7, the ATP/ADP ratio was reduced to 6.6 and 5.2 at 1 and 2 h, respectively. In the presence of 5 nM of T3, however, the ratio was maintained above the control level. A 1-h preincubation with rT3 dramatically augmented the reductions caused by elevated acidity. These reductions were completely reversed when the cells were incubated with T3.
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PMID:Adverse effects of reverse triiodothyronine on cellular metabolism as assessed by 1H and 31P NMR spectroscopy. 944 Jan 39

Archaea are the most extremophilic of the acidophilic microbes, combining, in many cases, acidophilicity with hyperthermophilicity. They form one of the three branches of the phylogenetic tree, and they are specifically found within the so-called crenarchaeota, typical members of which thrive at pH 1-3 and at temperatures of 75 degrees C to nearly 100 degrees C. Despite this, these cells can maintain a near neutral cytosol, and they use H+ for chemiosmotic coupling of ADP phosphorylation. These phenomena require efficient exclusion and disposal of protons. This is achieved by multiple synergistic mechanisms that act in parallel. One strategy is to use bipolar tetraether lipids as a matrix of their plasma membranes, providing low ion permeabilities, even at high temperatures. Additionally, an inverted membrane potential can help to balance a large pH gradient of up to 4 at a proton motive force of delta p = 140-180 mV. This is not a general rule, because in several species the membrane potential contributes only minimally. Also, local buffering capacity and charge profiles across the membrane may significantly influence adaptation to bulk phase acidity. Neither complex I nor complex III electron transport-coupled proton pump equivalents have been found in aerobic archaea. Only terminal oxidases seem to provide either H+ pumping or the generation of a proton gradient by chemical charge separation. Organization, redox centres and primary structures of some archaeal terminal quinol oxidase complexes are known and will be discussed. Much less is known about anaerobic sulfur reducers. For those a possible mechanism for proton exclusion is proposed.
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PMID:How can archaea cope with extreme acidity? 1020 17

Oxidative phosphorylation of isolated rat skeletal muscle mitochondria after exposure to lactic acidosis in either phosphorylating or nonphosphorylating states has been evaluated. Mitochondrial respiration and transmembrane potential (DeltaPsi(m)) were measured with pyruvate and malate as the substrates. The addition of lactic acid decreased the pH of the reaction medium from 7.5 to 6.4. When lactic acid was added to nonphosphorylating mitochondria, the subsequent maximal ADP-stimulated respiration decreased by 27% compared with that under control conditions (P < 0.05), and the apparent Michaelis-Menten constant (K(m)) for ADP decreased to 10 microM vs. 20 microM (P < 0.05) in controls. In contrast, maximal respiration and ADP sensitivity were not affected when mitochondria were exposed to acidosis during active phosphorylation in state 3. Acidosis significantly increased mitochondrial oxygen consumption in state 4 (post-state 3), irrespective of when acidosis was induced. This effect of acidosis was attenuated in the presence of oligomycin. The addition of lactic acid during state 4 respiration decreased DeltaPsi(m) by 19%. The ratio between added ADP and consumed oxygen (P/O) was close to the theoretical value of 3 in all conditions. The addition of potassium lactate during state 3 (i.e., medium pH unchanged) had no effect on the parameters measured. It is concluded that lactic acidosis has different effects when induced on nonphosphorylating vs. actively phosphorylating mitochondria. On the basis of these results, we suggest that the influence of lactic acidosis on muscle aerobic energy production depends on the physiological conditions at the onset of acidity.
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PMID:Actively phosphorylating mitochondria are more resistant to lactic acidosis than inactive mitochondria. 1044 5

Proton pumps of tonoplast membranes have been studied extensively in vitro, but data concerning their regulation in vivo are lacking. Effects of either anoxia, or the addition of KCN, 2-deoxy-d-glucose (deoxy-glucose), or bafilomycin-A1 (BAF) on vacuolar pH of maize (Zea mays L.) root hair cells were followed by fluorescence microscopy after loading of 2[prime]7[prime]-bis-(2-carboxyethyl)-5-(and-6) carboxyfluorescein. Root hair cells were able to maintain vacuolar acidity for at least 2 h in the presence of either 10 mM KCN or 50 mM deoxy-glucose or during anoxia. Treatments with either deoxy-glucose or KCN reduced total tissue ATP more than anoxia. ADP accumulated during anoxia and treatment with KCN as detected by in vivo 31P-NMR spectroscopy, but not during deoxy-glucose treatment. With control roots and roots treated with deoxy-glucose, the presence of BAF, a specific inhibitor of the V-type ATPase, caused alkalization of the vacuolar pH. However, either in the presence of KCN or under anoxic conditions, BAF was relatively ineffective in dissipating vacuolar acidity. Therefore, under anoxia or in the presence of KCN, unlike the situation with air or deoxy-glucose, the V-type ATPase apparently is not required for maintenance of vacuolar acidity.
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PMID:Effects of Bafilomycin A1 and Metabolic Inhibitors on the Maintenance of Vacuolar Acidity in Maize Root Hair Cells. 1222 44


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