The primary structure of the hemoglobin of the electric eel (Electrophorus electricus).
The blood of the Electric Eel contains only one hemoglobin component. The primary structures of the alpha- and beta-chains are presented. These were separated by high-performance liquid chromatography, using a new kind of buffer system. The alpha-chains are acetylated, and consist of 142 residues, while the beta-chains are not blocked, and consist of 147 residues. The phylogenetic distances between these and the alpha- and beta-chains of human hemoglobin are 48 and 50% amino-acid exchanges, respectively. The relationship between primary structure and the Bohr effect and Root effect is discussed, especially the significance of the serine found in position F9 beta.
Huber
F
F
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
Braunitzer
G
G
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004589:Electrophoresis, Disc; D004593:Electrophorus / Q000378:metabolism*; D004912:Erythrocytes / Q000032:analysis; D005914:Globins / Q000302:isolation & purification; D006454:Hemoglobins / Q000032:analysis*; D008969:Molecular Sequence Data
D000596:Amino Acids; D006454:Hemoglobins; D005914:Globins