The primary structure and oxygen-binding properties of the single haemoglobin of the high-Antarctic fish Aethotaxis mitopteryx DeWitt
The complete amino acid sequence of the single haemoglobin of the Antarctic fish Aethotaxis mitopteryx DeWitt has been established by automated repetitive Edman degradation on the intact and cleaved (enzymatically and chemically) α and β chains. A very high sequence identity with other Antarctic fish haemoglobins has been detected. The haemoglobin has a moderate Bohr effect and no Root effect. Organic phosphates and chloride also regulate oxygen binding only to a moderate extent. The lack of Root effect is consistent with the substitution His — Val at the HC3 C-terminal position of the β chain. The low overall heat of oxygenation suggests that in this species oxygen transport is an energy-saving process, presumably related to cold adaptation. The comparative analysis of the haemoglobins of Antarctic fishes emphasises some unique features of the oxygen-transport System of A. mitopteryx, which are likely to be related to its also rather unique mode of life.
KeywordsHPLC Enthalpy Acetonitrile Cysteine Trypsin
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- D’Avino R, Caruso C, Camardella L, Schininà ME, Rutigliano B, Romano M, Carratore V, Barra D, Prisco G di (1991) Anoverview of the molecular structure and functional properties of the hemoglobins of a cold-adapted Antarctic teleost. In: Prisco G di (ed) Life under extreme conditions. Biochemical adaptation. Springer, Berlin Heidelberg New York, pp 15–33Google Scholar
- Prisco G, di, D’Avino R, Caruso C, Tamburrini M, Camardella L, Rutigliano B, Carratore V, Romano R (1991) The biochemistry of oxygen transport in red-blooded Antarctic fishes. In: Prisco G di, Maresca B, Tota B (eds) Biology of Antarctic fish. Springer, Berlin Heidelberg New York, pp 263–281CrossRefGoogle Scholar
- Wells RMG, Jokumsen A (1982) Oxygen binding properties of hemoglobins from Antarctic fishes. Comp Biochem Physiol 71B:469–473Google Scholar