The primary structure of the hemoglobin of the Cormorant (Phalacrocorax carbo, Pelecaniformes).
The erythrocytes of the adult Cormorant contain two hemoglobin components in a ratio of 83% Hb A to 17% Hb D. The primary structures of the alpha A-, alpha D- and beta-chains are presented. The globin chains were separated by high-performance liquid chromatography and cleaved enzymatically and/or chemically. The native chains and their fragments were sequenced using liquid- or gas-phase sequencers, and the peptides aligned using the homology to human and to avian hemoglobin sequences. Compared to human hemoglobin, there are 46 amino-acid replacements in the alpha A-chains (67.4% homology), 65 replacements in the alpha D-chains (53.9% homology) and 45 replacements in the beta-chains (69.2% homology). In the functionally important regions, the percentage of amino-acid substitutions, as compared to human hemoglobin, is 13.2% in the alpha A-, 19.0% in the alpha D - and 16.0% in the beta-chains. The importance of the replacement beta 135 arginine (other birds)----glycine (Cormorant) in the phosphate-binding pocket and its effect on phosphate binding will be discussed.
Huber
K
K
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
Braunitzer
G
G
Schneeganss
D
D
Kösters
J
J
Grimm
F
F
D000595:Amino Acid Sequence; D000818:Animals; D001717:Birds / Q000097:blood*; D004912:Erythrocytes / Q000032:analysis; D006454:Hemoglobins / Q000302:isolation & purification; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification
D006454:Hemoglobins; D046911:Macromolecular Substances; D010446:Peptide Fragments