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1.
  • 1.1. The oxygen consumption rates for three sympatric species of marine gastrotrichs (anatomically similar, except that one contains hemoglobin) were measured with a Cartesian diver microrespirometer.
  • 2.2. The rates for the two species without hemoglobin, Turbanella ocellata and Dolichodasys carolinensis, were 307.2 μl O2 g−1 hr−1 and 108.0 μl O2 g−1 hr−1, respectively, while the rate for the hemoglobin-containing species, Neodasys, was 208.9 μl O2 g−1 hr−1.
  • 3.3. The possession of hemoglobin by Neodasys (14% by volume) cannot be explained by an unusually high demand for oxygen.
  • 4.4. Instead, the hemoglobin may be useful as an oxygen store providing continued aerobic metabolism in anoxic conditions, thus allowing Neodasys to exploit a different niche.
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2.
  • 1.1. Oxygen consumption was measured in a lemuriform prosimian, Cheirogaleus medius. throughout a 24-hr cycle. The standard metabolic rate was determined to be 0.95 ml O2 (g · hr)−1 agreeing well with the value predicted by allometric equations, 0.91 ml O2 (g · hr)−1.
  • 2.2. As a group, prosimians are argued to have metabolic levels in agreement with eutherian norms, rather than hypometabolic levels as previously supposed.
  • 3.3. Day length is shown to be an important behavioral cue for this species. Its complex yearly and daily torpor cycles are linked to this stimulus.
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3.
  • 1.1. Water efflux and urine production rates were measured in blue crabs acclimated to several salinities.
  • 2.2. In 100% seawater the mean rate of water efflux (31.3 ml/100g hr−1) was significantly greater than that in 50% seawater (18.9 ml/100 g hr−1.
  • 3.3. Water efflux was directly related to body weight.
  • 4.4. The mean urine production rate was significantly greater in crabs acclimated to 50% and 30% seawater (0.17 and 0.18 ml/100g hr−1) than in animals conditioned to 100% seawater (0.09 ml/100 g hr−1).
  • 5.5. The difference between theoretical net water fluxes for crabs exposed to 100% seawater and 50% seawater was similar to the difference in urine output in the same salinities, demonstrating the importance of the antennal gland in volume regulation.
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4.
  • 1.1. In late winter, oxygen consumption of honey bee (Apis mellifera L.) clusters showed marked 24-hr periodicity, even when held under constant temperature conditions.
  • 2.2. Minimal rates of metabolism (as low as 3.4 w kg −1) were usually reached at night (ca. 0500 hr), and maximum rates (as high as 33.5 w kg−1) in midday (ca. 1400 hr).
  • 3.3. Colonies with brood showed less excursion in daily metabolic rate, by maintaining higher night-time levels.
  • 4.4. There is a pronounced decrease in metabolic rate for the intact cluster of 9480–23,394 bees from the rates reported for individuals or small groups of bees.
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5.
  • 1.1. The thermal neutral zone of Cassin's Finches extends from 22 to 37.5°C.
  • 2.2. Standard metabolism (40.1 Wm−2 or 7.6kcal bird−1 day−1) of the 28 g birds was 89% of the value predicted for passerines measured at night.
  • 3.3. At temperatures below the zone of thermal neutrality metabolism is described by the relation, Wm−2 = 1.55–74.5°C. The coefficient of heat transfer (1.55Wm−2°C−1) is only 58% of the value predicted for birds of this size, indicating excellent insulation.
  • 4.4. At temperatures above thermal neutralzfsity metabolism is described by the relation, Wm−2 = 2.75–62.6°C.
  • 5.5. Under conditions of heat stress (44.5°C; PH2O = 8.6 Torr) Cassin's Finches were able to dissipate up to 208% of their metabolic heat production by evaporative water loss. Maximal rate of water loss was 56 mg g−1 hr−1.
  • 6.6. At 20°C resting fasted finches lost a mean of 4.94 ± 1.5 SD mg H2O g−1hr−1.
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6.
  • 1.l. High amino acid concentrations were found in the anterior coelomic fluid of a Polychaeta (Sabella pavonina Savigny).
  • 2.2. The concentrations being much higher in the fluid which penetrates the nephrostomia into the nephridia lumen than in the final urine indicates that the nephridia reabsorbs large amounts of amino acids.
  • 3.3. Nephridial perfusion experiments showed that an amino acid analogue (α-amino-iso-butyric acid, AIB) is transported by the nephidia.
  • 4.4. The transport took place across the nephridial wall owing to the presence of a carrier-mediated transport system and a diffusion system.
  • 5.5. For the carrier-mediated transport, the Vmax was 0.234 ± 0.025 nmol·min and the Km 3.715 ± 0.315mmol·l.
  • 6.6. AIB accumulated in the nephridial cells up to a maximum rate of 01.17 nmol·min.
  • 7.7. Intracellular accumulation stopped increasing when the Vmax for reabsorption was reached.
  • 8.8. These results indicate that the carrier-mediated transport of AIB is located at the apical membrane of the nephridial cell, and that AIB transport by simple diffusion takes place through the paracellular pathway.
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7.
  • 1.1. Changes in the blood and in the rate of oxygen consumption of Japanese eels injected intramuscularly in the head with a lethal dose of typical or atypical Aeromonas salmonicida at 20°C were investigated.
  • 2.2. Eels infected with the bacteria became moribund within 4 to 6 days, and then died within 1 day.
  • 3.3. The O2 consumption rate and blood parameters changed markedly with infections. The responses of hosts to infection by the two kinds of bacteria differed with regard to the following four points: blood pH, plasma Cl, lactic acid, and the numbers of granulocytes and lymphocytes.
  • 4.4. The responses of eels infected with atypical A. salmonicida were larger and more rapid than those of eels infected with typical A. salmonicida.
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8.
  • 1.1. The small intestine was cut into seven segments and properties and distribution of brush border Mg2+-HCO3-ATPase activity in each segment were examined.
  • 2.2. The optimal Mg2+ concentration was 1.0 mM.
  • 3.3. The optimal HCO3 concentration was 100 mM in the first (duodenal), 50 mM in the 3rd and 40 mM in the 5th segment, respectively.
  • 4.4. The optimal pH value was about 9.0.
  • 5.5. l-phenylalanine (above 1 mM) and SCN (above 50 mM) significantly inhibited both Mg2+- and Mg2+-HCO3-ATPase activity.
  • 6.6. The enzyme activity was found to be highest in the duodenal segment and then gradually decreased in consecutive segments as well as β-glycerophosphatase, Na+-K+-ATPase and supernatant carbonic anhydrase.
  • 7.7. The functional significance of this ATPase and the relationship with carbonic anhydrase was discussed.
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9.
  • 1.1. 14C-dichlorofarnesoate permeated rapidly into Haemonchus contortus (infective juveniles) and Panagrellus redivivus (mixed cultures) and was strongly bound by hydrophobic association (Ks > 10−4M).
  • 2.2. Uptake rose linearly with increases in temperature (5–38°C) and external concentration (C0; 0.07–2.15 × 10−4 M). Within 1 hr the internal concentration, C1 was >C C0.
  • 3.3. The pH of the medium (6–8) did not affect uptake.
  • 4.4. Efflux of dichlorofarnesoate was low: the half-time of release was > 18 hr.
  • 5.5. The uptake curve approximated to the expression C1/C0 = a(1 − e−bt) with a and b as constants and t in hr.
  • 6.6. These results clarify previous work on the inhibitory action of juvenile hormone on the development of nematodes.
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10.
  • 1.1. An endoxylanase (EC 3.2.1.8) was purified from an Escherichia coli strain carrying a xylanase gene from the extreme thermophile “Caldocellum saccharolyticum strain Tp8T6.3.3.1. It was found to have an Mr of 42,000 and an isoelectric point of approx. 5.0.
  • 2.2. The enzyme showed optimum activity at pH 5.0–7.7 and had an activation energy of 44 kJ mol−1. It was stable at room temperature at pH 4.5–11.5 in the presence of 0.5 mg ml−1 bovine serum albumin. The half-life of the enzyme at 75°C was 20 min at pH 6.0 in the presence of 0.5 mg ml−1 bovine serum albumin.
  • 3.3. The xylanase had highest activity on oat spelts xylan, releasing xylobiose and some xylotriose. The Km for oat spelts xylan was 0.021% (w/v) at pH6.0.
  • 4.4. The enzyme had high activity on sugar cane bagasse hemicelluloses A and B, lower activity on larchwood xylan and also hydrolysed carboxymethylcellulose, 4-methylumbelliferyl β-D-cellobioside and p-nitrophenyl β-D-cellobioside, but could not hydrolyse xylobiose.
  • 5.5. It showed transferase activity on p-nitrophenyl β-D-xylopyranoside. Xylose did not inhibit the enzyme.
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11.
  • 1.1. The mechanism of interaction of CP with O2 radicals in chemical and enzymatic systems of Superoxide radical generation as well as in the pulse radiolysis technique was studied.
  • 2.2. It is found that CP does not exert any kinetic influence on the decomposition of Superoxide radical and, unlike SOD, cannot catalyze the reaction of disproportionation of these radicals in systems with chemical and enzymatic generation of O2.
  • 3.3. The data obtained confirm the suggestion that CP interacts with precursors of 2 radicals.
  • 4.4. The irradiation of CP does not change its inhibiting activity in the reaction of the formation of Superoxide radicals in systems with enzymatic O2 generation, but decreases its oxidase activity.
  • 5.5. The results obtained demonstrated that the increase in the radiation dose resulted in the decrease of the inhibiting activity of SOD, whereas the activity of CP did not change.
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12.
  • 1.1. The purified enzyme hydrolyzes the linear l-lysinamide and the cycle amide of l-lysine—l-α-amino-ϵ-caprolactam.
  • 2.2. The apparent relative molecular mass is 180,000. The enzyme consists of four subunits and the molecular mass of a single subunit was found to be 47,000.
  • 3.3. The coefficient of molecular sedimentation equals 8.3 S, the isoelectric point was determined to be pH 4.3
  • 4.4. The enzyme is not a glycoprotein. p-Mercuribenzoate binds 10 SH-groups of the native enzyme molecule and 20 SH-groups in the presence of 0.7% SDS.
  • 5.5. pH- optimum for the hydrolysis of l-lysine amides was observed to be 7.5–7.7. The enzyme is strictly dependent on Mn2+ and Mg2+.
  • 6.6. The kinetic parameters for the hydrolysis of l-lysinamide where Km = 3.8 mM and kcat = 3000 sec−1 For the hydrolysis of cyclic L-lysinamide Km = 4.8 mM and kcat = 2600 sec.
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13.
  • 1.1. The ambient temperature of embryos of pipped eggs was reduced from 38 to 28°C for a period of 45 min.
  • 2.2. The blood PCO2 was lower and the blood more alkaline at 28°C than at 38°C.
  • 3.3. At 28°C plasma [HCO3] ] was lower than predicted from the blood buffer line determined in vitro.
  • 4.4. The plasma concentrations of strong ions and lactate were the same at both temperatures.
  • 5.5. After the ambient temperature had been returned to 38°C for a period of 45 min, blood pH was more acidic than before cooling, but there was no difference in blood PCO2.
  • 6.6. The plasma [HCO3] was the same as that at 28°C and plasma [K+] was higher than before cooling.
  • 7.7. The results arc discussed in relation to the factors affecting blood pH in embryos at this stage of development.
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14.
  • 1.1. The activation energy of the membrane bound H+-pyrophosphatase is 44.9 k J·mol−1, for the detergent solubilized enzyme is 55.9 kJ·mol−1.
  • 2.2. The Arrhenius plots obtained for pyrophosphatases of Rhodospirillum rubrum show no breaks.
  • 3.3. At 70°C, the membrane-bound pyrophosphatase is more stable in the presence of either Mg2+ or Zn2+ than in their absence.
  • 4.4. At 65°C, an activator effect of Mg2+ or Zn2+ was observed. Nevertheless, at 70°C no activation was obtained.
  • 5.5. The activator effects of Mg2+ or Zn2+ were depended of their concentration.
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15.
  • 1.1. The effect of short-term (79 hr) food deprivation at 27°C on body mass, locomotor activity, body temperature (Tb), and resting oxygen consumption was determined in eleven American kestrels (Falco sparverius).
  • 2.2. The change in body mass during resting followed the relation, % mass remaining = 99 e0.07(days fasting). There was no significant difference in the rate of relative mass loss between males and females.
  • 3.3. Locomotor activity, measured as perch hopping, was highly variable in both control and fasted birds and showed no correlation with stage of the fast, basal metabolic rate (BMR), or rate of mass loss during food deprivation.
  • 4.4. Body temperatures of fasted birds declined continuously by 0.2–0.4°C per day from 39.3 to 38.3°C.
  • 5.5. Both males and females responded to food deprivation with a decrease in metabolism. By the third night of fasting, BMR had declined 23.4% from 0.845 W (bird day)−1 to 0.647 W (bird day)−1. The observed reduction in BMR is 2.4 times that expected from a 1°C decline in Tb (assuming Q10 = 2.5) indicating active suppression of metabolism.
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16.
  • 1.1. The concentrations (mM) of osmolytes in the coelomic fluid of Luidia clathrata kept at 25‰S seawater (control individuals) were: 345, Na+; 10, K+; 10, Ca2+; 44, Mg2+; 387, Cl; 0.67, amino acids; 0.09, NH4+.
  • 2.2. When individuals were transferred from 25‰S to 15‰S or 35‰S, the concentrations of inorganic ions in the coelomic fluid usually equilibrated within 24hr and became the same as those in the medium.
  • 3.3. The intracellular water content (g intracellular H2O/g solute-free dry tissue) of the pyloric caeca and tube feet of control individuals throughout the experiment was 2.13 and 5.40, respectively.
  • 4.4. In tissues of individuals transferred to 15‰S, the intracellular water content increased by an average 50% in 12 hr but returned to 19% above control levels during 1 week.
  • 5.5. In tissues of individuals transferred to 35‰S, the intracellular water content decreased by an average 17% in 12 hr and did not change during 1 week.
  • 6.6. Luidia clathrata is an osmoconformer and partial cell volume regulator within the seasonal salinity range it encounters.
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17.
  • 1.1. Some aspects of the gas exchange system of a diving lizard, Physignathus lesuewii were studied.
  • 2.2. Breathing patterns were analysed.
  • 3.3. Breathing rate increases logarithmically with temperature and Q10 = 1.8. LogBR = −0.237 + 0.0256 T.
  • 4.4. Gas tensions in lung air and arterial and venous blood were measured. Arterial pH declines with increasing temperature.
  • 5.5. Temperature has a marked effect on oxygen affinity of the blood (ΔH = −10.1 kcal mol). A Bohr effect was also noted.
  • 6.6. CO2 equilibrium curves were drawn.
  • 7.7. The results are considered with a view to anticipating the efficiency of the gas exchange system of this species under conditions of variable temperature and during diving.
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18.
  • 1.1. The effects of extracellular pH on Na+ and Cl absorption were studied in vitro in the small intestine of the winter flounder, Pseudopleuronectes americanus.
  • 2.2. Reductions in bathing solution pH inhibited Jmsna (mucosal-to-serosal flux) and Jnetna (net flux) (r = 0.90) and JnetCl (r = 0.92) [due to an increase in JsmCl, (serosal-to-mucosal)] and decreased short circuit current (Isc).
  • 3.3. Luminal bumetanide (0.1 mM) and amiloride (1 mM) inhibited Na+ and Cl absorption by reducing Jms.
  • 4.4. Luminal barium (5mM) and luminal copper (100 μM) decreased JmsCl and increased JsmCl.
  • 5.5. We conclude that reductions in extracellular pH inhibit a luminal membrane NaCl absorptive process (Na+-K+-2Cl) and stimulate an electrogenic Cl secretory process.
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19.
  • 1.1. A standard procedure for lipid-extraction of lyophilized hen brain material is decribed.
  • 2.2. Nine carboxylesterase isoenzymes (EC 3.1.1.1) are identified in lipid-extracted lyophilized material (LELM) using kinetic analysis of organophosphate inhibition. Total phenyl valerate (PV) hydrolysing carboxylesterase activity in LELM is 43.3U.g−1
  • 3.3. Two carboxylesterase isoenzymes of LELM are classified as neurotoxic esterases (NTEA and NTEgB).
  • 4.4. Using n-octylglucoside 51% of the water-insoluble neurotoxic esterase activity from LELM are solubilized.
  • 5.5. Six carboxylesterase isoenzymes including NTEA (6.5 U-l−1) and NTEB (4.2 U-l−1) are present in the solubilized preparation.
  • 6.6. Throughout purification and separation steps carboxylesterase isoenzymes are identified by their rate constants for the reaction with organophosphorus inhibitors.
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20.
  • 1.1. The specific activity of Na-K ATPase was determined from the microsomal preparation of gills dissected from adult Macrobrachium rosenbergii.
  • 2.2. Maximal ATPase activity was achieved at a substrate concentration of 0.5 mM ATP.
  • 3.3. Optimal enzyme activity was obtained at pH of 7.5.
  • 4.4. The Arrhenius plot of Na-K ATPase activity revealed a marked discontinuity at 30°C. “Mg” ATPase activity did not exhibit a marked discontinuity.
  • 5.5. The Ea for Na-K ATPase and “Mg” ATPase was 14.6 kCal/mole and 9.31 kCal/mole respectively. Q10 values for Na-K ATPase was 2.34 and for “Mg” ATPase 1.65.
  • 6.6. ATPase activity and gill homogenate protein concentration exhibited a linear relationship up to 130 μg protein/ml.
  • 7.7. Na-K ATPase activity was inhibited by 10−3 M ouabain. It was equally inhibited by the removal of K+ from the reaction medium.
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