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The primary structure of hemoglobin from amur-leopard (Panthera pardus orientalis)

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The complete amino acid sequence of the major component of hemoglobin from amur-leopard (Panthera pardus orientalis) is presented. The major component accounts for more than 90% of the total hemoglobin. Separation of the globin subunits was achieved by ion-exchange chromatography on CM-cellulose in urea. The sequence was studied by automatic Edman degradation of tryptic and hydrolytic peptides. Alignment was carried out with human hemoglobin sequence. The β NH2 terminus is blocked with Ac-serine. The data are compared with other mammalian hemoglobins and results are discussed with respect to sequence and physiology.

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85th communication on hemoglobin.

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Abbasi, A., Braunitzer, G. The primary structure of hemoglobin from amur-leopard (Panthera pardus orientalis). J Protein Chem 4, 57–67 (1985). https://doi.org/10.1007/BF01025493

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  • DOI: https://doi.org/10.1007/BF01025493

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