Whole Blood–Oxygen Binding Properties of Four Cold‐Temperate Marine Fishes: Blood Affinity Is Independent of pH‐Dependent Binding, Routine Swimming Performance, and Environmental Hypoxia

2006 ◽  
Vol 79 (5) ◽  
pp. 909-918 ◽  
Author(s):  
Neill A. Herbert ◽  
Peter V. Skov ◽  
Rufus M. G. Wells ◽  
John F. Steffensen
Keyword(s):  
Whole Blood ◽  
Swimming Performance ◽  
Marine Fishes ◽  
Oxygen Binding ◽  
Blood Oxygen ◽  
Binding Properties ◽  
Environmental Hypoxia ◽  
Ph Dependent

Regulation of Blood Oxygen Affinity in the Australian Blackfish Gadopsis Marmoratus: I. Correlations between Oxygen-binding Properties, Habitat and Swimming Behaviour

1982 ◽  
Vol 99 (1) ◽  
pp. 223-243
Author(s):  
G. P. DOBSON ◽  
J. BALDWIN
Keyword(s):  
Whole Blood ◽  
Oxygen Affinity ◽  
Swimming Behaviour ◽  
Oxygen Binding ◽  
Blood Oxygen ◽  
Low Oxygen ◽  
Binding Properties ◽  
Molar Ratios ◽  
Blood Oxygen Affinity ◽  
Low Oxygen Affinity

1. The regulation of whole blood oxygen affinity in the freshwater blackfish Gadopsis marmoratus Richardson has been examined, and correlations made between oxygen-binding properties and the habitat and swimming behaviour of the fish. 2. Blackfish whole blood has a low oxygen affinity relative to other fish bloods reported in the literature. This is not due to a low oxygen affinity of the stripped haemoglobins, but arises from interactions between haemoglobin and intraerythrocytic modulators. 3. The presence of high concentrations of ATP, and to a lesser extent GTP, in the erythrocyte, together with the effect of these nucleoside triphosphates on the oxygen affinity of haemoglobin solutions at physiological NTP: Hb4 molar ratios, demonstrates that this class of compounds is a major regulator of oxygen affinity in blackfish blood. 4. The oxygen affinities of whole blood and haemoglobin solutions are sensitive to pH, with haemoglobin solutions displaying a relatively large alkaline Bohr coefficient of - 1.05 over the physiologically relevant pH range of 6.5–7.0. 5. Although increasing Pco2, lowers the oxygen affinity of whole blood, it does so only through the effect on pH, as pH-buffered haemoglobin solutions show no oxygen-linked CO2 binding. This lack of oxygen-linked CO2 binding has not been reported for any other naturally occurring vertebrate haemoglobins. 6. Muscle morphology and biochemistry, and behavioural observations, indicate that the blackfish uses anaerobic energy metabolism during rapid swimming and in recovery. 7. It is concluded that the oxygen-binding properties of blackfish blood reflect adaptations for maintaining adequate tissue oxygenation for animals at rest and during slow sustained swimming in waters of high oxygen tensions.

The blood oxygen binding properties of hypoxicSalmo gairdneri

1980 ◽  
Vol 136 (1) ◽  
pp. 83-87 ◽  
Author(s):  
Antti Soivio ◽  
Mikko Nikinmaa ◽  
Kai Westman
Keyword(s):  
Oxygen Binding ◽  
Blood Oxygen ◽  
Binding Properties

scholarly journals ALLOSTERIC CONTROL OF OXYGEN BINDING BY HAEMOGLOBIN DURING EMBRYONIC DEVELOPMENT IN THE CROCODILE CROCODYLUS POROSUS: THE ROLE OF RED CELL ORGANIC PHOSPHATES AND CARBON DIOXIDE

1993 ◽  
Vol 175 (1) ◽  
pp. 15-32 ◽  
Author(s):  
G. C. Grigg ◽  
R. M. G. Wells ◽  
L. A. Beard
Keyword(s):  
Embryonic Development ◽  
Whole Blood ◽  
Marked Effect ◽  
Oxygen Affinity ◽  
Oxygen Binding ◽  
Blood Oxygen ◽  
Embryonic Life ◽  
Crocodylus Porosus ◽  
Blood Oxygen Affinity ◽  
2,3 Dpg

The P50 of whole blood [30°C, PCO2=2.08 kPa (15.6 mmHg)] decreases during embryonic development from approximately 6.7 kPa (50 mmHg) at 15 days to about half this value at hatching (86 days), paralleling a decrease in ATP from 100 to 5–10 micromole g-1 Hb. There is also a progressive changeover from embryonic to adult haemoglobin (HbA). A pulse of 2,3- diphosphoglycerate (2,3-DPG) (18 micromole g-1 Hb) occurs late in embryonic life. It has no effect on whole-blood oxygen-affinity and falls rapidly at hatching to values typical of post-hatchling crocodilians in general (<1.0 micromole g-1 Hb). ATP has a marked effect on the oxygen affinity of embryonic haemoglobin (HbE) but not on HbA. 2,3-DPG has only very small effects on the oxygen affinities of HbE and HbA. CO2 has a small effect on the oxygen affinity of HbE but a marked effect on that of HbA. Values of PO2 measured in the chorio-allantoic artery [2.9 kPa (22 mmHg)] and vein [5.9 kPa (52 mmHg)] imply an increase in saturation from approximately 30 % to more than 80 %. Neither whole-blood oxygen-affinity nor ATP level was altered in response to an experimental 7-day exposure to low ambient oxygen levels [10.7 kPa (80 mmHg)]. The results do not lend themselves easily to the pan-selectionist paradigm in which all physiological traits are viewed as being adaptive.

THE INFLUENCE OF SALINITY ACCLIMATION ON THE TEMPERATURE SENSITIVITY OF OXYGEN BINDING TO THE HAEMOCYANIN OF THE PROSOBRANCH NEPTUNEA ANTIQUA

1990 ◽  
Vol 149 (1) ◽  
pp. 417-424 ◽  
Author(s):  
O. L. E. BRIX ◽  
SAVERIO G. CONDO ◽  
ALFREDO COLOSIMO ◽  
BRUNO GIARDINA
Keyword(s):  
Temperature Sensitivity ◽  
Whole Blood ◽  
Thermal Sensitivity ◽  
Ionic Concentration ◽  
Oxygen Binding ◽  
Salinity Acclimation ◽  
Ph Dependent

The thermal sensitivity of oxygen binding has been studied at 10, 15, 20 and 25 °C in whole blood from specimens of Neptunea antiqua acclimated to ambient salinities of 24 and 35‰. The O2 affinity is strongly pH-dependent, demonstrating a large reversed Bohr shift below pH8.0. The magnitude of the Bohr shift is not significantly influenced by temperature or ionic concentration. At 35‰, the blood O2-affinity is strongly influenced by temperature (δHapp-≈58.6kJmol−1), while at 24‰ there is almost no temperature sensitivity (δHapp<-18.8kJmol−1)

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

1976 ◽  
Vol 65 (2) ◽  
pp. 333-345 ◽  
Author(s):  
R. E. Weber ◽  
S. C. Wood ◽  
J. P. Lomholt
Keyword(s):  
Rainbow Trout ◽  
Whole Blood ◽  
Relative Concentration ◽  
Oxygen Affinity ◽  
Temperature Acclimation ◽  
Organic Phosphate ◽  
Red Cells ◽  
Oxygen Binding ◽  
Binding Properties

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.

Blood–oxygen binding in healthy Standardbred horses

2005 ◽  
Vol 169 (2) ◽  
pp. 251-256 ◽  
Author(s):  
C. Cambier ◽  
N. Di Passio ◽  
T. Clerbaux ◽  
H. Amory ◽  
V. Marville ◽  
...  
Keyword(s):  
Oxygen Binding ◽  
Blood Oxygen
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