Primary structure of the hemoglobin beta-chain of rose-ringed parakeet (Psittacula krameri).
The primary structure of Rose-ringed Parakeet hemoglobin beta-chain was established, completing the analysis of this hemoglobin. Comparison with other avian beta-chains show variations smaller than those for the corresponding alpha-chains. There are 11 amino acid exchanges in relationship to the only other characterized psittaciform beta-chain, and a total of 35 positions are affected by differences among all avian beta-chains analyzed (versus 61 for the alpha-chains). At three positions, the Psittacula beta-chain has residues unique to this species. Three alpha 1 beta 1 contacts are modified, by substitutions at positions beta 51, beta 116, and beta 125.
Islam
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Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden.
Persson
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Zaidi
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Jörnvall
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D000595:Amino Acid Sequence; D000818:Animals; D006454:Hemoglobins / Q000032:analysis* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010240:Parakeets / Q000097:blood*; D011563:Psittaciformes / Q000097:blood*; D013045:Species Specificity
D006454:Hemoglobins