The primary structure and oxygen-binding properties of the single haemoglobin of the high-Antarctic fish Aethotaxis mitopteryx DeWitt |
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Authors: | Rossana D'Avino Angela Fago Andreas Kunzmann Guido di Prisco |
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Affiliation: | (1) Institute of Protein Biochemistry and Enzymology, C.N.R., Via Marconi 10, I-80125 Naples, Italy;(2) Institut für Polarökologie, Universität Kiel, Olshausenstrasse 40-60, W-2300 Kiel, Germany |
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Abstract: | 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) and 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 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 |
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