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

During a one-year period of treatment, the authors found indications for (hemangioma, tattoos, viral warts) and limits of CO2 laser therapy (nevus flammeus, keloid).
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PMID:[Experiences with the CO2 laser in dermatology]. 640 71

Laboratory white rats and fossorial mole rats (Spalax ehrenbergi) were subjected to progressive hypoxia by enclosure in a thermoregulated, confined atmosphere. Variable levels of environmental CO2 were obtained by controlling the duration of CO2 absorbance. Rats had preimplanted electroencephalographic (EEG) and electrocardiographic (EKG) electrodes and a rectal temperature probe. Animals were followed until their last gasp and EEG flattening, at which time the chamber's atmosphere was analyzed. The mole rat demonstrated a significantly lower terminal PIO2 [20.9 +/- 3.5 (SD) vs. 38.0 +/- 8.4 (SD) Torr]; however, in both animals terminal PIO2 was independent of PICO2 over a range of the latter of 0-117 Torr. Rats showed a progressive decline in rectal temperature from a PIO2 of 80 Torr on, amounting finally to 2.3 degrees C. The rats' oxygen consumption was maintained down to a PIO2 of 65 Torr and declined from then on. A group of rats with maximal CO2 accumulation showed a greater decline of rectal temperature and a steeper drop of VO2 with respect to PO2 compared to a group with no CO2 buildup. The main result was unexpected, in view of the theoretical synergism of the adverse effects of hypoxia and hypercapnia, and should reorient current thinking on survival and resuscitation in confined spaces.
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PMID:Independence of hypoxic death of inspiratory PCO2 in rats and fossorial mole rats. 643 55

Streptococcus bovis H13/1 was grown in a glucose-limited chemostat. A concomitant increase in dilution rate and glucose supply per unit time caused both an increase in lactate production per mole of glucose fermented and a linear increase in growth yield over the dilution rate range 0.052 to 0.141/h. When the dilution rate was increased with no change in glucose supply per unit time there was a reduction in lactate production and an increase in that of acetate and ethanol coinciding with a non-linear increase in growth yield. YMaxglu = 38.6 and a maintenance coefficient, ms = 0.290 mmol/l glucose/g cells/h were calculated. The results also suggested an interaction between the formate and CO2 pools.
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PMID:Changes in metabolism of the rumen bacterium Streptococcus bovis H13/1 resulting from alteration in dilution rate and glucose supply per unit time. 650 Nov 21

When isolated rat pancreatic islets are exposed to L-leucine (20 mM), the rate of NH4 production is close to the summed rates of L-[1-14C] leucine decarboxylation and alpha-ketoisocarproate production, whereas the rates of acetoacetate production and L-[U-14C]-leucine oxidation are compatible with conversion of each mole of the amino acid to one mole of acetoacetate and three moles of CO2. ATP content, ATP/ADP ratio, and adenylate charge are maintained at normal values by L-leucine, whereas the NADH/NAD+ ratio (but not the NADPH/NADP+ ratio) is significantly increased. The release of insulin evoked by L-leucine is potentiated by 2-ketoisovalerate, unaffected by L-valine, and inhibited by menadione. L-leucine mimicks the effect of D-glucose on 86Rb+ and 45Ca2+ handling by the islets. However, relative to its rate of oxidation, the insulinotropic effect of L-leucine is less marked than that of D-glucose. This may be due, in part at least, to a decrease in the oxidation of endogenous nutrients. It is concluded that the metabolic, cationic, and secretory effects of L-leucine in isolated islets are not incompatible with the fuel hypothesis for insulin release.
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PMID:The stimulus-secretion coupling of amino acid-induced insulin release: metabolism and cationic effects of leucine. 676 28

The influence of temperature on the oxygeneration of normal and 2,3-diphosphoglycerate-depleted human blood suspensions (final hemoglobin concentration: 0.75%) was studied under closed-system conditions (constant total CO2 content) beginning with standard values:pH 7.40, Pco2 40 torr, at 37 degrees C. The present results quantify the temperature-induced changes in Po2 occuring in association with the concomitant acid-base variations prevailing in a closed system. When the temperature was raised from 25 to 42 degrees C, P50 varied from 13.9 +/- 1.1 to 40.7 +/- 1.9 torr in the presence of 2,3-DPG and from 7.6 +/- 0.4 to 24.8 +/- 1.2 torr in the absence of the cofactor. The derived equations correlate Po2 variations with those of temperature (T: 25--42 degrees C) and oxygen saturation (So2:10--90%). The temperature coefficient of oxygenation and the DPG-induced decrease in the heat of hemoglobin oxygenation were shown to be saturation dependent. DPG lowered dlog Po2/dT from 0.0299 to 0.0275 and delta H from --12.9 to --11.8 kcal/mole O2 bound at 50% So2 but had no significant influence on these parameters for So2 less than or equal to 20%. The results suggest that the release of carbamate at the beginning of oxygenation is virtually unaffected by presence of 2,3-DPG in the 25--42 degree C temperature range.
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PMID:Temperature and oxygenation of human blood at constant total CO2 content. 677 81

An acyl coenzyme A (CoA) carboxylase, which catalyzes the adenosine triphosphate-dependent fixation of CO2 into acetyl-, propionyl-, and butyryl-CoA, was detected in fractionated cell extracts of Propionibacterium shermanii. Catalytic activity was inhibited by avidin but was unaffected by avidin pretreated with excess biotin. The carboxylase levels detected were relatively small and were related to cellular growth. Maximal carboxylase activity was detected in cells grown for about 96 h. Thereafter, the activity declined rapidly. Optimal CO2 fixation occurred at pH 7.5. Other parameters of the assay system were optimized, and the apparent Km values for substrates were determined. The end product of the reaction (with acetyl-CoA as the substrate) was identified as malonyl-CoA. The stoichiometry of the reaction was such that, for every mole of acetyl-CoA and adenosine triphosphate consumed, 1 mol each of malonyl-CoA, adenosine diphosphate, and orthophosphate was formed. These data provide the first evidence for the presence of another biotin-containing enzyme, an acyl-CoA carboxylase, in these bacteria in addition to the well-characterized methylmalonyl-CoA carboxyltransferase.
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PMID:Acyl coenzyme A carboxylase of Propionibacterium shermanii: detection and properties. 679 64

The relationship between acid-base status and temperature was studied in the channel catfish, Ictalurus punctatus. The change in blood pH with temperature had a slope of -0.0132/degrees C and involved both a decrease in total CO2 at higher temperatures, and a significant rise in arterial PCO2. The acid-base changes in the intracellular compartment were similar to those in the blood, except that for red and white muscle the slope of the change in pH with temperature had a slightly higher value (-0.0185 and -0.0147, respectively), and for heart muscle it had a smaller value (-0.0117). The net whole-body excretion of acid or base in response to temperature change was relatively small: 0.40 m-mole . kg-1 net OH- was excreted in response to an increase from 22 to 31 degrees C, and 0.31 m-mole . kg-1 net H+ was excreted in response to change from 25 to 15 degrees C. In both cases approximately half was excreted renally and half branchially. Using information on the volumes and buffer capacities of the various body fluid compartments as well as the information above, the ratio of imidazole to phosphate intracellular buffers was calculated to be 5.1 to 1. The amount of intercompartmental (active) transfer required to make temperature adjustments is strongly dependent on the buffer ratio, and on the PCO2. Without the observed changes in PCO2 with temperature, the transfer requirement would have been 3 to 4 times larger.
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PMID:Intracellular and extracellular acid-base status as a function of temperature in the freshwater channel catfish, Ictalurus punctatus. 681 17

In order to understand the mechanism responsible for the high oxygen affinity of mole blood, we investigated in the mole. Talpa europaea, red cell parameters that determine hemoglobin function. We have found that the oxygen half saturation pressure (P50) of mole blood is 2.85 kPa (21.4 Torr) at pCO2 4.7 kPa, pH 7.4 and 37 degree C. The concentration of 2,3-diphosphoglycerate (2,3-DPG) averaged 5.3 mmol/l in red cells. In addition, we have determined P50 in hemoglobin solutions at various concentrations of 2,3-DPG at an assumed intraerythrocytic pH of 7.2 and 37 degree C. These data were used to calculate the association constants of 2,3-DPG to mole hemoglobin. P50 was 1,89 kPa (14.2 Torr) in hemoglobin solutions without 2,3-DPG. The response to 2,3-DPG was relatively low. Noteworthy, CO2 did not affect the oxygen affinity at constant pH in the presence of 2,3-DPG. Our results suggest that the high blood oxygen affinity of the mole can be attributed to a weak interaction of its hemoglobin with 2,3-DPG.
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PMID:Adaptation of hemoglobin function to subterranean life in the mole, Talpa europaea. 733 Apr 93

Anion exchange across the red cell membrane was studied by measuring the rate of shrinkage of cells when transferred from a medium of low pH to one of higher pH. Removal of trace amounts of CO2/bicarbonate from the media by degassing and the inhibition of carbonic anhydrase with 5 microM ethoxzolamide slowed the shrinkage rate. Arrhenius plots were linear over a temperature range of 40 degrees C, both in the presence of trace amounts of CO2/bicarbonate and in their absence, and gave an apparent activation energy for Cl- exchange of 73.9 +/- 8.9 kJ mole-1 when CO2 was present but this increased to 135.8 +/- 7.7 kJ mole-1 in its absence. From the results it is concluded that the lower value for the activation energy is determined by the rate of formation of bicarbonate ions while the high value represents hydroxyl:anion exchange and is a truer measure of the activation energy of the exchange process.
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PMID:Effect of carbon dioxide on the temperature dependence of anion exchange in human red cells. 749 39

The effects of methanol addition and consumption on chloroform degradation rate and product distribution in methanogenic methanol enrichment cultures and in cultures of Methanosarcina barkeri 227 were investigated. Degradation of chloroform with initial concentrations up to 27.3 microM in enrichment cultures and 4.8 microM in pure cultures was stimulated by the addition of methanol. However, methanol consumption was inhibited by as little as 2.5 microM chloroform in enrichment cultures and 0.8 microM chloroform in pure cultures, suggesting that the presence of methanol, not its exact concentration or consumption rate, was the most significant variable affecting chloroform degradation rate. Methanol addition also significantly increased the number of moles of dichloromethane produced per mole of chloroform consumed. In enrichment cultures, the number of moles of dichloromethane produced per mole of chloroform consumed ranged from 0.7 (methanol consumption essentially uninhibited) to 0.35 (methanol consumption significantly inhibited) to less than 0.2 (methanol not added to the culture). In pure cultures, the number of moles of dichloromethane produced per mole of chloroform consumed was 0.47 when methanol was added and 0.24 when no methanol was added. Studies with [14C]chloroform in both enrichment and pure cultures confirmed that methanol metabolism stimulated dichloromethane production compared with CO2 production. The results indicate that while the addition of methanol significantly stimulated chloroform degradation in both methanogenic methanol enrichment cultures and cultures of M. barkeri 227, the prospects for use of methanol as a growth substrate for anaerobic chloroform-degrading systems may be limited unless the increased production of undesirable chloroform degradation products and the inhibition of methanol consumption can be mitigated.
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PMID:Chloroform degradation in methanogenic methanol enrichment cultures and by Methanosarcina barkeri 227. 757 27


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