The Primary Structure of Electric Ray Hemoglobin(Torpedo marmorata).Bohr Effect and Phosphate Interaction

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Abstract
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 .fwdarw. Lys is significant, while the mutations .beta.2 His .fwdarw. Ser, .beta.82 Lys .fwdarw. Asn and .beta.142 His .fwdarw. Cys are important for the lack of effector affinity.