PubMed Health⌕ Search

Biomedical subjects

R E Weber

Publications and source records attributed to R E Weber.

At least 91 records · Page 5Linked to original sources
PubMed1977

Blood respiratory properties of rainbow trout (Salmo gairdneri) kept in water of high CO2 tension.

1. Blood O2 transport and acid-base balance were studied at 20 degrees C in rainbow trout (Salmo gairdneri) which had been kept in water of high CO2 content (15 mmHg) for at least a week. Also the blood gas chemistry of fish rapidly entering or leaving the hypercapnic environment was studied. 2. Fish entering high CO2 water suffered a sharp decrease in blood pH which significantly reduced O2 transport by the blood, but after a few hours considerable compensation was achieved. 3. After at least a week in high CO2 water, trout showed elevated plasma bicarbonate and PCO2 levels, and a decrease in plasma chloride, while pH was about 0 - 1 pH unit below the level for control fish. Oxygen transport by the blood was marginally reduced. 4. Hypercapnic fish rapidly entering fresh water showed a sharp increase in blood pH and a decrease in blood PO2. These parameters regained normal values after a few hours but plasma bicarbonate and chloride levels took much longer to regain control concentrations. 5. Acid-base balance in hypercapnic fish is discussed with particular reference to the role of the branchial ion exchanges.

Adaptation, Physiological↗
PubMed1977

pH and haemoglobin oxygen affinity in blood from the Antarctic cod Dissostichus mawsoni.

Blood pH in the antarctic cod (Dissostichus mawsoni) and in two Trematomus species, occlrring at --1-9 degrees C, is extremely high (approximately 8-2 to 8-3). This supports and extends Rahn's (1966) model for the temperature-pH relationship in cold-blooded vertebrates. The blood of D. mawsoni shows a low oxygen affinity (P50 approximately equal to 14-5 mmHg at pH 8-16 and -1-9 degrees C). Despite normal in vitro temperature and pH sensitivities, blood P50 increases only slightly when live fish are temperature-stressed (+ 4-0 degrees C), or become acidotic as a result of agitational stress (blood pH 7-71), primarily as a result of compensatory decreases in blood ATP levels. Oxygen-binding properties of 'stripped' (cofactor-free) solutions of D. mawsoni haemoglobin were measured in attempts to elucidate the molecular mechanisms involved in the function of the pigment.

Adenosine Triphosphate↗
PubMed1976

The hemoglobin system of the primitive fish, Amia calva: isolation and functional characterization of the individual hemoglobin components.

Blood from the primitive holostean fish, the bowfin, Amia calva, contains 2 mo of ATP per mol of hemoglobin. The hemolysates contain at least five tetrameric hemoglobin components which differ in their oxygen affinities and their response to cofactors such as ATP. The binding of oxygen by each chromatographically isolated component, including a cathodal component, is influenced by pH and organic phosphates; there is no significant differentiation of function or structure as seen in trout and certain other fish hemolysates. Kinetic analyses of ligand binding indicate that the Bohr and Root effects of Amia calva hemoglobins are best explained by changes in both the "on" and "off" constants. At low pH, the increase in the "off" constant is smaller than for most other Root hemoglobins. The hemoglobin system of Amina calva is functionally undifferentiated and may be representative of the ancestral condition in teleosts.

Animals↗
PubMed1976

Blood respiratory properties in the naked mole rat Heterocephalus glaber, a mammal of low body temperature.

Respiratory properties of whole blood and Hb solutions have been studied in Heterocephalus glaber, a fossorial rodent, having a low body temperature (30.0-32.0 degrees C) and poor thermoregulatory ability. For comparison similar, measurements were made on laboratory mice, Mus musculus. Whole blood showed a distinctly higher O2 affinity for Heterocephalus at both 30 and 37 degrees C.P50 values were 23.3 mm Hg and 33.0 mm Hg at 37 degrees C for Heterocephalus and Mus, respectively, while at 30 degrees CP50's were 18.8 mm Hg and 24.9 mm Hg, all values at pH (b) 7.4. deltaH values (expressive of the effect of temperature on P50) were -5.8 kcal-mol-1 for Heterocephalus and -7.5 kcal-mol-1 for Mus. The CO2 Bohr effects (omega) were -0.43 and -0.50 for Heterocephalus at 37 and 30 degrees C. Corresponding values for Mus were -0.65 and -0.56. Both species had a Hill's n-value of 2.6. Red cell concentrations of 2,3-DGP were closely similar in the species being 7.3 mmol-L-1 rbc for Heterocephalus and 7.4 mmol-L-1 rbc for Mus. Stripped Heterocephalus Hb had a very high O2 affinity, at pH 7.25, 37 degrees C,P50 was 8.0 mm Hg whereas the corresponding value for Mus was 11.3 mm Hg. Addition of DPG to stripped Hb from the two species decreased O2 affinity to the same degree. The high O2 affinity of Heterocephalus blood is viewed as a possible adaptation to its burrowing habits. Its basis is inherent to the hemoglobin molecule itself and not dependent upon cofactor influence or the temperature sensitivity of the O2-Hb binding.

Adaptation, Physiological↗
PubMed1976

Respiratory properties of blood in awake and estivating lungfish, Protopterus amphibius.

Blood respiratory properties have been studied in awake and estivating African lungfish, Protopterus amphibius. Fish had been estivating 28-30 months when blood was sampled. Hematocrit, O2 capacity and blood hemoglobin concentration increased by about 50% during estivation. Red cell Hb concentration (MCHC) was unaltered. Total blood concentration of nucleoside triphosphates (NTP) was reduced 50% in estivation. Thin-layer chromatography showed that the change in NTP resulted from a GTP/Hb (guanosine triphosphate) reduction to 20% of the value in awake fish. ATP (adenosine triphosphate) concentration remained largely unaltered. GTP/Hb changes were accompanied by marked changes in O2 affinity. The P50 value in blood from awake fish was 33 mm Hg at pH 7.5 compared to 9 mm Hg for the estivating fish. The n-value changed insignificantly. An increased Bohr effect was present in estivating fish, but its importance will depend on circulating pH in the two states. Standard bicarbonate ranged from a low of 8.6 mMol-L-1 (P plasma) at pH 7.5 in an awake fish to 49.6 mMol-L-1 (P) in an estivating fish. CO2 dissociation curves showed a variable Haldane effect having its highest value in the in vivo range of PCO2. The striking increase in O2-Hb affinity during estivation is regarded as an adaptation to a reduced alveolar O2 availability associated with estivation. Altered mechanics of pulmonary ventilation and reduced ambient O2 availability caused by the subterranean habitat may have been selection pressures for the development of the high O2 availability caused by the subterranean habitat may have been selection pressures for the development of the high O2 affinity. The mechanism behind it rests with the recorded change in erythrocytic concentration of GTP.

Adaptation, Physiological↗
PubMed1976

Physiological properties of eel haemoglobin: hypoxic acclimation, phosphate effects and multiplicity.

Unlike the whole body oxygen affinity, which adapts readily to environmental oxygen tensions, haemoglobins, prepared from normoxic- and hypoxic-accimated eels (Anguilla anguilla) show no adaptive changes in oxygenation properties or in multiplicity. Hypoxic acclimation is, howeveer, accompanied by a strong decrease in red cell nucleoside triphosphates, particularly guanosine triphospphate (GTP), which depresses oxygen affinity of the composite and component haemoglobins more strongly than does the concurring ATP. The effects of pH, temperature and salts on the oxygenation properties of the (isolated) haemoglobins are reported, discussed in relation to the varying environmetal conditions encountered by eels, and compared with data on American and Japanese eels (A. rostrata and A. juponica, respectively.

Adenosine Triphosphate↗
PubMed1976

Temperature acclimation and oxygen-binding properties of blood and multiple haemoglobins of rainbow trout.

Acclimation of rainbow trout to 5, 15 and 22 degrees C for periods exceeding 4 months had no significant effect on the oxygen affinity of whole blood or on the concentration of ATP, which is the main organic phosphate in red cells. Slight differences were, however, found in the oxygenation properties of the haemolysates, which correlate with changes in the relative concentration of the multiple haemoglobins. The oxygen-binding properties of the main haemoglobin components account for the observed differences in the haemolysates. The possible thermoacclimatory significance of changes in haemoglobin multiplicity and co-factor concentrations is discussed.

Adaptation, Physiological↗
PubMed1975

Effects of ambient PO2 on hemoglobin-oxygen affinity and red cell ATP concentrations in a benthic fish, Pleuronectes platessa.

Previous studies have demonstrated that acclimation of mammals and fish to hypoxic conditions elicits opposite responses in red cell organic phosphate levels (an increase and a decrease, respectively). This investigation focuses on the "reverse" response - when the benthic fish Pleuronectes platessa, which occurs locally under hypoxic conditions, is subjected to higher oxygen tensions. Compared to the hypoxic (PO2 =30 mm Hg) situation the ATP:Hb ratio in increased (1.1 to 1.8) and oxygen affinity is increased (i.e. P50 changed from 18 to 30 mm, at pH 7.7 and 15 degrees C) by acclimation to Po2 of 150 mm Hg. Under hyperoxic conditions (Po2 =300 mm Hg) the ATP:hemoglobin ratio and blood P50 showed a surprising decrease and returned to values comparable to those in hypoxic fish (to 1.3 and 18 mm Hg, respectively). When "stripped" of organic and inorganic ions hemoglobin solutions prepared from fish acclimated at 30 and at 150 mm Hg have the same P50 and Bohr effect values, showing that the intra-erythrocytic factor rather than changes in the hemoglobin molecules, are involved. The pure hemoglobin shows high sensitivity to ATP at physiological concentrations. There is evidence that apart from the direct helcotropic effects, ATP decreases oxygen affinity in the red cells through modification of the Donnan distribution of protons across the red cell membrane. Fish acclimated to 30 and 150 mm Hg oxygen tensions showed the same oxygen consumption rates at the same oxygen tensions.

Acclimatization↗
PubMed1975

Oxygen uptake and blood respiratory properties of the caecilian Boulengerula taitanus.

In contrast to amphibians belonging to the orders Urodela and Anura, virtually no data exist on the respiratory physiology of the more primitive Apoda. This study concerns oxygen uptake and hemoglobin function in the caecilan Boulengerula taitanus, an apodan with fossorial habits. The oxygen uptake rate resembles that of other amphibians of similar size. The blood was high O2 capacity (14 vol%) and the erythrocytes are smaller, and the red cell count is greater than in other amphibians. The oxygen affinity of whole blood is high compared to other amphibians (P50 = 28 mm Hg at 25 degrees C and pH 7.6). The oxygen equilibrium curve is sigmoid (n = 1.79) and the Bohr factor is small (deltalog P50/deltapH = - 0.21). In 'stripped' hemoglobin solutions oxygen affinity increases strongly (P50 = 3.3 mm Hg at 25 degrees C and pH 7.6) and the temperature sensitivity is high (apparent deltaH=-19.4 kcal/mole), but the ATP and pH influences are too low to account for the difference in P50 compared to whole blood. The high oxygen capacity and oxygen affinity and the low Bohr factor may have adaptive significance to this fossorial amphibian.

Adenosine Triphosphate↗