The primary structure of electric ray hemoglobin (Torpedo marmorata). Bohr effect and phosphate interaction.
The blood of the Electric Ray contains a number of hemoglobin components. The primary structures of the alpha- and beta-chains of the main components are presented. These chains were purified by high-performance liquid chromatography, using a new buffer system. The alpha-chains consist of 141 residues, and the beta-chains of 142 residues; both are unblocked. The phylogenetic distances from human alpha- and beta-chains are 55% and 64% amino-acid exchanges, respectively. The relationship between primary structure and the lack of both a Bohr effect and any effector affinity is discussed, and interpreted on a molecular level with reference to the sequence presented. For the Bohr effect, the mutation beta 89 Asp----Lys is significant, while the mutations beta 2 His----Ser, beta 82 Lys----Asn and beta 142 His----Cys are important for the lack of effector affinity.
Huber
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Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
Braunitzer
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D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D006454:Hemoglobins / Q000032:analysis*; D008969:Molecular Sequence Data; D010710:Phosphates; D014101:Torpedo / Q000097:blood*
D006454:Hemoglobins; D010710:Phosphates