Primary structure of the hemolglobin β-chain of Rose-ringed Parakeet (Psittacula krameri)

descriptionPublicationkeyboard_double_arrow_right Article 01 Aug 1989 English Publisher:Springer Science and Business Media LLCJournal:Journal of Protein Chemistry, volume 8, pages 481-486 (issn: 0277-8033, eissn: 1573-4943,

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Authors: A, Islam; B, Persson; Z H, Zaidi; H, Jörnvall;

doi: 10.1007/bf01026432

pmid: 2803513

Primary structure of the hemolglobin β-chain of Rose-ringed Parakeet (Psittacula krameri)

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Abstract

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.

Related Organizations

Karolinska Institute
Sweden
International Center for Chemical and Biological Sciences
Pakistan
University of Karachi
Pakistan

Keywords

Hemoglobins, Species Specificity, Molecular Sequence Data, Parakeets, Animals, Amino Acid Sequence, Psittaciformes

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