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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The microbiological oxidation of ferrous ion and the extraction of uranium from a low-grade ore has been studied using an adapted strain of Thiobacillus ferrooxidans. The effect of temperature, pH, volumetric oxygen transfer coefficient, K1a, and aeration number, Ia, on the activity of the microorganism has been determined. The activation energy for ferrous iron oxidation was calculated to be - 13.9 +/- 0.1 kcal/mole and inactivation (thermal death of bacteria) 53.3 +/- 0.2 kcal/mole. Temperature coefficient, Q10, was estimated to be 1.8. Uranium extraction varied between 80 and 100%.
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PMID:[Ferrous ion oxidation and uranium solubilization from a lowgrade ore by "Thiobacillus ferrooxidans" (author's transl)]. 0 31

The S-adenosyl-methionine: catechol-O-methyltransferase (EC 2.1.1.6) from rat kidney was purified about 650 fold as compared with the homogenate and the result of disc electrophoresis presented. The purification involved extraction, precipitation at pH 5, ammonium sulfate fractionation, Chromatographies on Biogel 0.5 m, Ultrogel AcA 44 and DE Sephadex A 50. Affinity chromatography was tried but unsuccessful. The enzyme exhibited two pH optima at 7.9 and 9.6 with a minimum at about 8.9. The COMT had a temperature optimum of 50 degrees C, with activation energy of 23.1 Kcal/Mole between 25-35 degrees C, 18.9 Kcal/mole between 35-45 degrees C and the Q10 within the range of 25-35 degrees amounted to 3.5. The molecular weight was estimated to be 21500+/-1000 daltons from its behavior on Ultrogel AcA 44 and the pH1 determined by electrofocalisation was near 5.50. The time of half life of the best purified enzymatic extract was found to be 2 h 10 min. at -20 degrees C. At basic pH the instability of the enzyme was increased. Since O-methylation required the presence of divalent cations, our results show that apparent Michaelis constants for Mg++ and Mn++ were respectively 0.50 X 10(-3) M and 0.33 X 10(-5) M. The study of their Hill's number indicated that there was only one point of fixation on the enzyme. The Km value determined by Florini and Vestling's method were 2.5 X 10(-4) M and 11.9 X 10(-5) M for epinephrine and S-adenosyl-methionine respectively. All results were discussed with respect to other investigations.
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PMID:[Purification and properties of rat kidney catechol-O-methyltransferase]. 1 36

Transport of L-glycine by the haustorial mycoparasite Tieghemiomyces parasiticus grown in axenic culture was investigated using endogenously metabolizing cells. Transport occurred against a concentration gradient and required the expenditure of energy supplied by metabolic reactions that were inhibited by catalytic amounts of sodium azide and 2,4-dinitrophenol. The process exhibited both pH and temperature dependence with optima at pH 4 and 35 degrees C, respectively. The energy of activation and Q10 for transport were calculated to be 18,227 cal/mole and 2.82 respectively, between 20 and 30 degrees C. The kinetics of the system were consistent with a mechanism of transport that depended upon a finite number of sites on the cell surface and had a Kt of 1.46 x 10(-5) M. The system for L-glycine transport lacked sterospecificity and was most inhibited in the presence of other neutral amino acids while less inhibition was observed in the presence of the acidic and basic amino acids. These results suggest that L-glycine transport in this mycoparasite occurs by an energy dependent, protein-mediated process characteristic of active transport.
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PMID:Transport of 14C-L-glycine by the haustorial mycoparasite Tieghemiomyces parasiticus in axenic culture. 2 97

1. The characteristics of saxitoxin (STX) binding to the mammalian Na channel have been studied in purified sarcolemma isolated from rat skeletal muscle. 2. STX binds specifically to isolated sarcolemma with a Kd of 1.43 x 10(-9) M and Bmax of 7-8 p-mole STX bound/mg membrane protein at 0 degrees C in the presence of 140 mM-NaCl. In rat muscle homogenate under the same conditions the corresponding values are Kd = 1.53 x 10(-9) M and Bmax = 0.15-0.20 p-mole/mg protein (18-20 p-mole/g wet wt.). Membrane purification produced a fortyfold increase in STX binding site concentration per milligram protein. Calculated binding site density in isolated sarcolemma was about 30 sites/micron 2 of membrane surface. 3. Denervation (10-14 days) results in a 43% reduction in the density of high-affinity STX binding sites in purified sarcolemma, but the Kd for this class of sites is not changed. 4. In sarcolemma, the apparent Kd for STX binding is dependent on temperature pH and ionic strength. The Q10 for Kd between 0 and 40 degrees C is 1.3. Protonation of a group having a pK of 6.0 markedly raises Kd without affecting Bmax. Apparent Kd increases eightfold when ionic strength is raised from 20 to 600 mM. 5. Dissociation and association rate constants for STX binding are temperature dependent with Q10 of 2.6 and 1.9 respectively between 0 and 20 degrees C. 6. STX binding is competitively inhibited by monovalent and divalent cations under conditions of constant total ionic strength. An affinity sequence of Tl+ greater than Li+ greater than Na+ greater than K+ greater than Rb+ greater than Cs+ is seen for the monovalent cation-binding site. 7. The STX binding site is relatively stable to heat and to enzymic degradation. A specific modifier of carboxyl residues inactivates subsequent STX binding. This process can be prevented by the presence of STX during the reaction. 8. Characteristics of the STX binding site in isolated sarcolemma are compared to those reported for other isolated excitable membranes and for studies of whole muscle and muscle homogenate. Sarcolemma provides a potential source of enriched Na channels for further purification efforts in a mammalian system.
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PMID:Characteristics of saxitoxin binding to the sodium channel of sarcolemma isolated from rat skeletal muscle. 4 83

1. Tissue oxygen uptake and enzyme activities were investigated in the naked mole rat, Heterocephalus glaber, a mammal notable for its low body temperature and metabolism and poor temperature regulating ability. 2. Q10 for O2 uptake of Heterocephalus crude liver homogenates ranged from 1.91 for the temperature interval 25-30 degrees C to 1.76 within the range 30-38 degrees C, values similar to those reported for typical homoiotherms. 3. Km pyruvate of lactate dehydrogenase in heart muscle had the same temperature dependence in the mole rat and mouse. 4. O2 uptake and cytochrome oxidase activity of skeletal muscle were higher for mole rat than mouse. The reverse was true for heart muscle. Brain and liver O2 uptake showed similar values for both species, while kidney O2 uptake was highest in the mouse. 5. Pyruvate kinase activity in heart and skeletal muscle was higher in mouse than mole rat, suggesting a greater reliance on glycolysis in the former. 6. Na+, K+ -ATPase activity of liver and kidney was 60% higher in mouse than mole rat, while brain was 30% higher in mouse. 7. The results indicate that the effects of temperature on tissue metabolism in the mole rat conform to those in typical homoiotherms. The low body temperature and O2 uptake in the mole rat find no expression in the tissue respiratory capacity.
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PMID:Tissue metabolism and enzyme activities in the rodent Heterocephalus glaber, a poor temperature regulator. 23 74

1. The influence of internal and external Na concentrations on Ca movements have been measured in pinch-off presynaptic nerve terminals (synaptosomes). Ca uptake is enhanced when external Na (Nao) is replaced by Li, choline or dextrose, in Na-loaded synaptosomes. Depletion of internal Na (Nai) abolishes the stimulatory effect of external Na removal. 2. Ca uptake from Na-depleted media is proportional to [Na]i -2, and averages about 1-5 mumole Ca/g synaptosome protein per minute when [Na]i is approximately 137 mM. This may correspond to a Ca influx of about 0-1 p-mole/cm-2 sec. 3. External Na is a competitive inhibitor of the Nai-dependent Ca uptake. The interrelationship between [Na]o, [Ca]o and Ca uptake indicate that two external Na ions may compete with one Ca at each uptake site. 4. The distribution of particles with Nai-dependent Ca uptake activity parallels the distribution of synaptosomes in the preparative sucrose gradient. Thus, this Ca uptake activity is probably a property of the pinched-off nerve terminals per se, and not of the mitochondria which may contaminate the synaptosome fraction. 5. The Nai-dependent Ca uptake mechanism requires an intact surface membrane, since synaptosomes subjected to osmotic lysis lose the ability to accumulate Ca by this route. 6. Ca efflux into Ca-free media is largely dependent upon the presence of external Na. The curve relating Ca efflux to [Na]o is sigmoid, and suggests that more than one external Na ion (perhaps 2 or 3) is needed to activate the efflux of each Ca ion. 7. The net Ca gain exhibited by Na-loaded synaptosomes incubated in Na-depleted media can be accounted for by the increased Ca uptake and decreased Ca loss observed under these conditions. 8. Treatment of synaptosomes with cyanide or 2,4-dinitrophenol decreases Ca uptake and enhances Ca efflux into Na-containing media. This results in a net loss of Ca from the terminals, even in the presence of external Ca. 9. In contrast to the Ca efflux from synaptosomes, the Ca efflux from brain mitochondria is not dependent upon external Na, and is reduced by succinate, a substrate which is known to fuel mitochondrial respiration. 10. The temperature coefficient (Q10) of the Nai-dependent Ca uptake is about 3. 11. The Nai-dependent Ca uptake is reduced at low pH. The relationship between this Ca uptake and pH approximates a titration curve with a pKa of about 5-6. 12. The data indicate that Ca transport in rat brain presynaptic terminals may involve a carrier-mediated Na-Ca exchange mechanism, and that some of the energy required for Ca extrusion may come from the Na electrochemical gradient across the surface membranes.
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PMID:The influence of sodium on calcium fluxes in pinched-off nerve terminals in vitro. 23 34

Ribulose-diphosphate carboxylase from Thiobacillus novellus has been purified to hemogeneity as observed by polyacrylamide gel electrophoresis and U.V. light observation during sedimentation velocity analysis. The optimum pH for the enzyme with Tris-HCl buffers was about 8.2. Concentrations of this buffer in excess of 80 mM were inhibitory. The apparent Km for RuDP was about 14.8 muM with a Hill value of 1.5, for HCO3- the apparent Km was about 11.7 mM with an n value of 1.18 and for Mg2+ about 0.61 mM. The enzyme was specific for this cation. Relatively high concentrations of either Hg2+ or pCMB were required before significant inhibition was observed. Activity declined slowly during a 4-hr incubation period in either 3.0 M or 8.0 M urea. Incubation for 12 hrs resulted in complete loss of activity which was not prevented by 10 mM Mg2+ and was not reversed by dialysis and subsequent addition of 10 mM cysteine. Polyacrylamide gel electrophoresis revealed a loss of the major band and the appearance of 2 new bands. SDS polyacrylamide gel electrophoresis gave an average M.W. of 73500 +/- 2500 for the slower moving band and 12250 +/- 2500 for the faster moving. However, incubation in urea for up to 40 hrs revealed a decrease in the M.W. of the slower moving band to about 60000. The Ea for the enzyme was calculated to be about 18.85 kcal mole-1, with the possibility of a "break" between 40 and 50 degrees C. The Q10 was 3.07 between 20 and 30 degrees C whereas between 30 to 40 degrees C it was 3.31. Only phosphorylated compounds caused significant inhibition of enzyme activity. They included ADP, FDP, F6P, G6P, PEP, 6PG, 2-PGA, R1P, R5P, and Ru5p.
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PMID:Properties and regulation of ribulose diphosphate carboxylase from Thiobacillus novellus. 24 94

Measurements of the temperature dependence in the range from 10 C to 30 C on the passive and dynamic electrical properties of single frog muscle cell following Arrhenius relation have been made. The propagated responses (V-t) and conduction velocity theta were analyzed following the H-H propagated cable equation. The ionic current-membrane potential relationship (I-t) was calculated from the phase-plane trajectory analysis (V-V) of the action potential curve (V-t). All the rate and time constants of the excitation and propagation processes kr, kNa, kK, tau Na, tau K, the negative conductance (-gNa) and the ionic conductances gNa, gK, influencing the evolution of the curves (V-t), (V-V) and (I-V) are correlated. The magnitudes of the resting (Vr) and action potential amplitude (Vs), the excitation potential (V*), the negative after potential (Vn), and the sodium equilibrium potential (VNa); the magnitudes of the maximum rate of rise and fall of the spike (V+) and (V-) and those corresponding to the inward INa and outward IK ionic currents, were analyzed. Two general classes of findings were obtained. One group of action potential parameters theta, V+, V-, Vn, kr, kNa, kK, tau Na, tau K, -gNa, gNa, gK, INa and IK is strongly temperature dependent with Q 10 S approximately 2 and energy of activation E approximately 10 kcal/mole. The other group of parameters, Gm (passive conductance), Cm (capacitance), tau, Vr, V*, Vs, and VNa are slightly temperature dependent, with Q10's lower than 1.4. This study contributes deeply to the analysis of temperature effects on the electrical cell responses to adequate stimuli. This temperature dependence analysis was designed to detect possible "masked" actions of microwave radiation on cell membrane functions.
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PMID:Temperature dependence on the passive and dynamic electrical parameters of muscle cells. 31 91

This study was an attempt to observe the effects of temperature on adsorption and one-step growth of the virus N-1 infecting the nitrogen-fixing cyanobacterium Nostoc muscorum. Adsorption rate was found to maximum at 40 degrees C whereas no adsorption occurred at 10 degrees C. The Q10 value was about 2.03 and the energy of activation, Ea was 16.3 kcal/mole for the adsorption process. The development cycle of the virus was temperature sensitive. With increase in temperature, a gradual increase in inhibition of virus yield i.e. 8.33% at 30 degrees C, 35.3% at 35 degrees C and complete inhibition at 40 degrees C was observed. Out of 7 h latent period, the early 4 h were temperature sensitive and heat treatment had a reversible inhibitory effect on virus development. The temperature treatment did not affect the rise period but burst-size was reduced.
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PMID:Effect of temperature on the adsorption and one-step growth of the Nostoc virus N-1. 41 22

1. The reversal potential for the pace-maker K current, iK2, was measured in sheep cardiac Purkinje fibres at extracellular K concentrations, [K]O, between 2-7 and 8 mM. The reversal potentials were found to be significantly more negative than the values predicted using the Nernst equation for any reasonable value of intracellular K+ concentration or activity. 2. It is suggested that this discrepancy may be explained by postulating that the extracellular K+ concentration [K]e in the cleft spaces between cells is smaller than [K]o as a result of ion pumping and restricted diffusion from the bulk extracellular medium. 3. In conformity with this hypothesis, it was shown that the value of [K]e may be further reduced by hyperpolarizing pulses, presumably as a consequence of K+ depletion during the passage of inward current. 4. The influence of temperature on the kinetics of the gating mechanism, s, controlling iK2 was investigated. The Q10 for the time constant, pis, of current change following voltage clamp steps was found to be about 17. This corresponds to an apparent activation enthalpy of 50 kcal/mole. 5. The Q10 of the maximum amplitude iotaK2, was found to 1-3. 6. The activation curve, s infinity (Em), spread slightly to more negative potentials by cooling from 37 to 30 degrees C and the curve became less steep. 7. There is a large decrease in the inward background current on cooling, as estimated by measuring the net membrane current when iK is presumed to be zero, i.e. at the reversal potential for iK2.
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PMID:The effects of potassium and temperature on the pace-maker current, iK2, in Purkinje fibres. 96 78


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