The amino acid sequence and oxygen-binding properties of single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps

Sapienza University of Rome, Roma, Latium, Italy
Archives of Biochemistry and Biophysics (Impact Factor: 3.02). 02/1992; 292(1):295-302. DOI: 10.1016/0003-9861(92)90082-8
Source: PubMed


The complete amino acid sequence of the single hemoglobin of the Antarctic teleost Gymnodraco acuticeps has been determined. The alpha chain contains 142 amino acid residues; an acetylated seryl residue is at the amino terminal. The beta chain contains 146 residues. A very high degree of sequence identity has been found with hemoglobins of other Antarctic fishes. Oxygen binding is not modulated by pH and allosteric effectors. The Bohr and Root effects are absent, although specific amino acid residues, considered responsible of most of these functions, are conserved in the sequence, thus posing new questions about the molecular basis of these mechanisms. The low heat of oxygenation may be interpreted as one of the mechanisms involved in the process of cold adaptation.

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    • "In detail, alkylation of thiol groups with 4-vinylpyridine and deacylation of the a-chain N terminus were carried out as described previously (D'Avino & di Prisco, 1989; Tamburrini et al., 1992, 1996). Alkylated globins were purified by reverse-phase HPLC, on a C4 Vydac column (4.6 9 250 mm). "
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