Sea snake (Microcephalophis gracilis) hemoglobin: Primary structure and relationships to other forms |
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Authors: | alia Islam Bengt Persson Zafar H Zaidi and Hans J?rnvall |
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Institution: | (1) Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden;(2) Center for Biotechnology, Huddinge University Hospital, S-141 86 Huddinge, Sweden;(3) HEJ Research Institute of Chemistry, University of Karachi, Karachi-32, Pakistan |
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Abstract: | The hemoglobin of the sea snakeMicrocephalophis gracilis was purified and the primary structure of the and chains determined. This is the first sea snake hemoglobin structure characterized, and apparently also the first complete structure of any snake hemoglobin (an chain of a viper was known), allowing judgments of reptilian variants. Variations between the sea snake form and other reptilian forms are large (52–65 differences for the chains), of similar order as those between the sea snake and avian (56–65 differences) or human (58 differences) forms. Functionally, 19 residues at / contact areas and 7 at heme contacts are exchanged in relation to the human and chains. Four positions of the sea snake hemoglobin contain residues thus far unique to this form. However, all replacements appear compatible with conserved overall functional properties. |
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Keywords: | Hemoglobin sea snake amino acid sequence structure-function relationships reptile relationships |
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