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Biomed Biochim Acta. 1983;42(6):685-95.

[The primary structure of hemoglobins from the bottlenosed dolphin (Tursiops truncatus, Cetacea)].

[Article in German]


Only one hemoglobin component was found in the bottlenosed dolphin (Tursiops truncatus, Cetacea). The alpha and beta chains were separated by chromatography on CM-52 cellulose. The complete primary structures of both chains were established by automatic Edman degradation of the chains and the tryptic peptides. The alignment was done by homology with alpha und beta chains of adult human hemoglobin. A comparison of these two hemoglobins shows an exchange of 22 amino acid residues in the alpha chains and of 20 in the beta chains which corresponds to the phylogenetic distance between primates and cetacea. In the surroundings of the heme we found one substitution in the beta chains. In the alpha 1 beta 1 subunit interphase three and four residues are exchanged respectively in the alpha and beta chains. The possible influence of two exchanges in the alpha 1 beta 2 contact region (alpha 38 (C3) Thr leads to Ser and alpha 44 (CD2) Pro leads to Ser) on the oxygen affinity is discussed. Compared with hemoglobins of terrestrial mammals the primary structure of dolphin hemoglobin shows no amino acid substitutions, which alter the function of the molecule significantly. The adaptation to hypoxic conditions during diving is regulated by other mechanisms.

[Indexed for MEDLINE]

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