The primary structure and oxygen-binding properties of the single haemoglobin of the high-Antarctic fish Aethotaxis mitopteryx DeWitt

1992 ◽  
pp. 135-140
Author(s):  
Rossana D’Avino ◽  
Angela Fago ◽  
Andreas Kunzmann ◽  
Guido di Prisco
Keyword(s):  
Primary Structure ◽  
Antarctic Fish ◽  
Oxygen Binding ◽  
Binding Properties

The primary structure and oxygen-binding properties of the single haemoglobin of the high-Antarctic fish Aethotaxis mitopteryx DeWitt

Polar Biology ◽  
1992 ◽  
Vol 12 (1) ◽  
pp. 135-140 ◽  
Author(s):  
Rossana D'Avino ◽  
Angela Fago ◽  
Andreas Kunzmann ◽  
Guido di Prisco
Keyword(s):  
Primary Structure ◽  
Antarctic Fish ◽  
Oxygen Binding ◽  
Binding Properties

Primary Structure and Oxygen-Binding Properties of the Hemoglobin from the Lesser Hedgehog Tenrec(Echinops telfairi,Zalambdodonta). Evidence for Phylogenetic Isolation

1991 ◽  
Vol 372 (2) ◽  
pp. 975-990 ◽  
Author(s):  
Marco PICCININI ◽  
Traute KLEINSCHMIDT ◽  
Thomas GORR ◽  
Roy E. WEBER ◽  
Heinz KÜNZLE ◽  
...  
Keyword(s):  
Primary Structure ◽  
Oxygen Binding ◽  
Binding Properties

Antarctic fish hemoglobin: an outline of the molecular structure and oxygen binding properties—II. Oxygen binding properties

1988 ◽  
Vol 90 (3) ◽  
pp. 585-591 ◽  
Author(s):  
Guido Di Prisco ◽  
Bruno Giardina ◽  
Rossana D'Avino ◽  
Saverio G. Condò ◽  
Andrea Bellelli ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Antarctic Fish ◽  
Oxygen Binding ◽  
Binding Properties ◽  
Fish Hemoglobin

Primary Structure and Oxygen-Binding Properties of the Hemoglobin from Guanaco (Lama guanacoë,Tylopoda)

1990 ◽  
Vol 371 (2) ◽  
pp. 641-648 ◽  
Author(s):  
Marco PICCININI ◽  
Traute KLEINSCHMIDT ◽  
Klaus D. JÜRGENS ◽  
Gerhard BRAUNITZER
Keyword(s):  
Primary Structure ◽  
Oxygen Binding ◽  
Binding Properties

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.

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