Abstract
The structure of the hernoglobin α-chain of Rose-ringed Parakeet was determined by sequence degradations of the intact subunit, the CNBr fragments, and peptides obtained by digestion with staphylococcal Glu-specific protease and trypsin. Using this analysis, the complete α-chain structure of 21 avian species is known, permitting comparisons of the protein structure and of avian relationships. The structure exhibits differences from previously established avian α-chains at a total of 61 positions, five of which have residues unique to those of the parakeet (Ser-12, Gly-65, Ser-67, Ala-121, and Leu-134). The analysis defines hemoglobin variation within an additional avian order (Psittaciformes), demonstrates distant patterns for evaluation of relationships within other avian orders, and lends support to taxonomic conclusions from molecular data.
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Islam, A., Beg, O.U., Persson, B. et al. Primary structure of the hemoglobin α-chain of rose-ringed parakeet (Psittacula krameri). J Protein Chem 7, 561–569 (1988). https://doi.org/10.1007/BF01024874
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DOI: https://doi.org/10.1007/BF01024874