Summary
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.
Data presented here were collected during the European Polarstern Study (EPOS) sponsored by the European Science Foundation
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Barra D, Petruzzelli R, Bossa F, Brunori M (1983) Primary structure of hemoglobin from trout (Salmo irideus). Amino acid sequence of the β-chain of trout Hb I. Biochim Biophys Acta 742:72–77
Bossa F, Barra D, Petruzzelli R, Martini F, Brunori M (1978) Primary structure of hemoglobin from trout (Salmo irideus). Amino acid sequence of α-chain of Hb trout I. Biochim Biophys Acta 536:298–305
Brauer AW, Oman CL, Margolies MN (1984) Use of o-phthalaldehyde to reduce background during automated Edman degradation. Anal Biochem 137:134–142
Brunori M (1975) Molecular adaptation to physiological requirements: The hemoglobin System of trout. Curr Top Cell Regul 9:1–39
Caruso C, Rutigliano B, Romano M, Prisco G di (1991) The hemoglobins of the cold-adapted Antarctic teleost Cygnodraco mawsoni. Biochim Biophys Acta 1078:273–282
D’Avino R, Prisco G di (1989) Hemoglobin from the Antarctic fish Notothenia coriiceps neglecta. 1. Purification and characterization. Eur J Biochem 179:699–705
D’Avino R, Caruso C, Romano M, Camardella L, Rutigliano B, Prisco G di (1989) Hemoglobin from the Antarctic fish Notothenia coriiceps neglecta. 2. Amino acid sequence of the α chain of Hb 1. Eur J Biochem 179:707–713
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 15–33
Friedman M, Krull LH, Cavins JF (1970) The chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl) cysteine. J Biol Chem 245:3868–3871
Giardina B, Amiconi G (1981) Measurement of binding of gaseous and nongaseous ligands to hemoglobins by conventional spectro-photometric procedures. Methods Enzymol 76:417–427
Hirs CHW (1967) Performic acid oxydation. Methods Enzymol 11:197–199
Kunzmann A, Caruso C, Prisco G di (1991) Haematological studies on a high-Antarctic fish: Bathydraco marri Norman. J Exp Mar Biol Ecol 152:243–255
Kunzmann A, Fago A, D’Avino R, Prisco G di (1992) Haematological studies on Aethotaxis mitopteryx DeWitt, a high-Antarctic fish with a single haemoglobin. Polar Biol 12:141–145
Landon M (1977) Cleavage at aspartyl-prolyl bonds. Methods Enzymol 47:145–149
Perutz MF, Brunori M (1982) Stereochemistry of cooperative effects in fish and amphibian haemoglobins. Nature 299:421–426
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 263–281
Qvist J, Weber RE, DeVries AL, Zapol WM (1977) pH and haemoglobin oxygen affinity in blood from the Antarctic cod Dissostichus mawsoni. J Exp Biol 67:77–88
Rossi Fanelli A, Antonini E, Caputo A (1958) Studies on the structure of hemoglobin. I. Physiocochemical properties of human globin. Biochim Biophys Acta 30:608–615
Shih TB, Jones R, Bonaventura J, Bonaventura C, Schneider RG (1984) Involvement of His HC3(146)β in the Bohr effect of human hemoglobin. J Biol Chem 259:967–974
Tamburrini M, Brancaccio A, Ippoliti R, Prisco G di (1992) The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps. Arch Biochem Biophys 292:295–302
Wells RMG, Jokumsen A (1982) Oxygen binding properties of hemoglobins from Antarctic fishes. Comp Biochem Physiol 71B:469–473
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1992 Springer-Verlag
About this paper
Cite this paper
D’Avino, R., Fago, A., Kunzmann, A., di Prisco, G. (1992). The primary structure and oxygen-binding properties of the single haemoglobin of the high-Antarctic fish Aethotaxis mitopteryx DeWitt. In: Hempel, G. (eds) Weddell Sea Ecology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-77595-6_15
Download citation
DOI: https://doi.org/10.1007/978-3-642-77595-6_15
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-77597-0
Online ISBN: 978-3-642-77595-6
eBook Packages: Springer Book Archive