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

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.

Blood oxygen binding properties for the burrowing owl,Athene cunicularia

1989 ◽  
Vol 76 (2) ◽  
pp. 205-214 ◽  
Author(s):  
Leigh A. Maginniss ◽  
Delbert L. Kilgore
Keyword(s):  
Oxygen Binding ◽  
Blood Oxygen ◽  
Athene Cunicularia ◽  
Binding Properties ◽  
Burrowing Owl

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

scholarly journals Haemoglobin polymorphisms affect the oxygen-binding properties in Atlantic cod populations

2008 ◽  
Vol 276 (1658) ◽  
pp. 833-841 ◽  
Author(s):  
Øivind Andersen ◽  
Ola Frang Wetten ◽  
Maria Cristina De Rosa ◽  
Carl Andre ◽  
Cristiana Carelli Alinovi ◽  
...  
Keyword(s):  
Evolutionary Biology ◽  
Quaternary Structure ◽  
Atlantic Cod ◽  
Three Dimensional ◽  
Oxygen Affinity ◽  
Oxygen Binding ◽  
Low Oxygen ◽  
Binding Properties ◽  
Important Species ◽  
The North

A major challenge in evolutionary biology is to identify the genes underlying adaptation. The oxygen-transporting haemoglobins directly link external conditions with metabolic needs and therefore represent a unique system for studying environmental effects on molecular evolution. We have discovered two haemoglobin polymorphisms in Atlantic cod populations inhabiting varying temperature and oxygen regimes in the North Atlantic. Three-dimensional modelling of the tetrameric haemoglobin structure demonstrated that the two amino acid replacements Met55β 1 Val and Lys62β 1 Ala are located at crucial positions of the α 1 β 1 subunit interface and haem pocket, respectively. The replacements are proposed to affect the oxygen-binding properties by modifying the haemoglobin quaternary structure and electrostatic feature. Intriguingly, the same molecular mechanism for facilitating oxygen binding is found in avian species adapted to high altitudes, illustrating convergent evolution in water- and air-breathing vertebrates to reduction in environmental oxygen availability. Cod populations inhabiting the cold Arctic waters and the low-oxygen Baltic Sea seem well adapted to these conditions by possessing the high oxygen affinity Val55–Ala62 haplotype, while the temperature-insensitive Met55–Lys62 haplotype predominates in the southern populations. The distinct distributions of the functionally different haemoglobin variants indicate that the present biogeography of this ecologically and economically important species might be seriously affected by global warming.

Effects of chronic hypobaric hypoxia on blood oxygen binding in pigeons

1997 ◽  
Vol 277 (4) ◽  
pp. 293-300 ◽  
Author(s):  
Leigh A. Maginniss ◽  
Marvin H. Bernstein ◽  
Mark A. Deitch ◽  
Berry Pinshow
Keyword(s):  
Hypobaric Hypoxia ◽  
Oxygen Binding ◽  
Blood Oxygen
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