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

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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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Authors and Affiliations

  1. HEJ Research Institute of Chemistry, University of Karachi, 75270, Karachi, Pakistan

    Chand Sultana, Atiya Abbasi & Zafar H. Zaidi

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  1. Chand Sultana
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  2. Atiya Abbasi
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  3. Zafar H. Zaidi
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Sultana, C., Abbasi, A. & Zaidi, Z.H. Primary structure of hemoglobin β-chain fromColumba livia (gray wild pigeon). J Protein Chem 10, 145–149 (1991). https://doi.org/10.1007/BF01024777

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  • DOI: https://doi.org/10.1007/BF01024777

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