Abstract
We determined the complete amino acid sequences of the Erabu sea snake (Laticaudia semifasciata) hemoglobin by analyzing the intact globin chains, enzymatically digested fragments, and chemical cleavage fragments to clarify the molecular evolution and phylogenetic classification of the sea snake. The Erabu sea snake has two types of hemoglobin components, Hb-I and Hb-II, which contain different α- and β-chains. This is the second report of the complete primary structure for hemoglobin of snakes. The sequences were compared with those of other reptilian hemoglobins. Amino acids at positions critical for the structure and physiological functions of hemoglobin were loosely conserved. The requirements for binding of ATP and of diphosphoglycerate as allosteric effectors of β-globins seemed to be fulfilled.
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Eguchi, Y., Eguchi, T. Amino Acid Sequence of the α- and β-Globin Chains of the Erabu Sea Snake (Laticaudia semifasciata). J Protein Chem 22, 489–497 (2003). https://doi.org/10.1023/B:JOPC.0000005465.95477.70
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DOI: https://doi.org/10.1023/B:JOPC.0000005465.95477.70