Primary structure of hemoglobin β-chain fromColumba livia (gray wild pigeon)

Abstract
Primary structure of β-chain of pigeon is presented. It was determined by amino acid sequence analysis of intact β-chain and its peptides obtained by the enzymatic and chemical cleavage. Comparison of amino acid sequence of the chain with other available data shows β 14 Ile, β61 Lys, and β113 Ile as residues specific to pigeon. One important replacement at α1β1 contact is β55 Met→Ser.

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