Abstract
The primary structure of Rose-ringed Parakeet hemoglobin β-chain was established, completing the analysis of this hemoglobin. Comparisons with other avian β-chains show variations smaller than those for the corresponding α-chains. There are 11 amino acid exchanges in relationship to the only other characterized psittaciform β-chain, and a total of 35 positions are affected by differences among all avian β-chains analyzed (versus 61 for the α-chains). At three positions, the Psittacula β-chain has residues unique to this species. Three α1β1 contacts are modified, by substitutions at positions β51, β116, and β125.
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Islam, A., Persson, B., Zaidi, Z.H. et al. Primary structure of the hemolglobin β-chain of Rose-ringed Parakeet (Psittacula krameri). J Protein Chem 8, 481–486 (1989). https://doi.org/10.1007/BF01026432
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DOI: https://doi.org/10.1007/BF01026432