Amino acid sequence of the alpha- and beta-globin chains of the Hiroo sea snake (Laticauda laticaudata)

We determined the hemoglobin complete amino acid sequences of the Hiroo sea snake (Laticaudia laticuada) from the intact globin chain, enzymatically digested fragments, and chemical cleavage fragments to analyze molecular evolution for classification of the sea snake. The Hiroo sea snake has two hem...

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Bibliographic Details
Published in:Journal of Protein Chemistry 2002-03, Vol.21 (3), p.215-221
Main Authors: Eguchi, Yukinori, Eguchi, Tomoko
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Allosteric properties
Amino Acid Sequence
Amino acids
Animals
Aquatic reptiles
Chromatography, Ion Exchange
Diphosphoglyceric Acids - metabolism
Elapidae - blood
Evolutionary biology
Fragments
Globins - chemistry
Globins - isolation & purification
Globins - metabolism
Hemoglobin
Hemoglobins - chemistry
Hemoglobins - metabolism
Marine
Molecular biology
Molecular evolution
Molecular Sequence Data
Reptilian Proteins - blood
Reptilian Proteins - chemistry
Reptilian Proteins - isolation & purification
Snakes
Structure-Activity Relationship
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Summary:We determined the hemoglobin complete amino acid sequences of the Hiroo sea snake (Laticaudia laticuada) from the intact globin chain, enzymatically digested fragments, and chemical cleavage fragments to analyze molecular evolution for classification of the sea snake. The Hiroo sea snake has two hemoglobin components, Hb-I and Hb-II, which contain different alpha- and beta-chains, respectively. This is the first report of the complete primary structure of a snake hemoglobin. The sequences were compared with those of other reptilian hemoglobins. Amino acid replacements at positions critical for structure and physiological role of hemoglobin were loosely conserved. The requirements for binding of ATP and of diphosphoglycerate as allosteric effectors at beta-globins seemed to be fullfilled.
ISSN:0277-8033
1572-3887
1573-4943
DOI:10.1023/A:1015333018932