The Primary Structure of the Hemoglobin of the Electric Eel(Electrophorus electricus).

Abstract
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 chromatogrpahy, 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.

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