Carnivora: primary structure of the hemoglobin from the spotted hyena (Crocuta crocuta, Hyenidae).
The primary structure of the alpha- and beta-chains of hemoglobin from spotted hyena (Crocuta crocuta, Hyenidae) is presented. The structure-function relationship is discussed. The separation of the chains directly from hemoglobin was performed by RP-HPLC. After tryptic digestion of the chains, the peptides were isolated by RP-HPLC. Amino-acid sequences were determined by Edman degradation in liquid- and gas-phase sequencers. The alignment of the tryptic peptides was made by homology with human and other Carnivora hemoglobins. The hemoglobin from spotted hyena (Crocuta crocuta) exhibits in its alpha- and beta-chains 22 and 20 exchanges, respectively, compared to human hemoglobin. In the alpha-chains, two alpha 1 beta 1-contacts are exchanged. In the beta-chains five exchanges involve one alpha 1 beta 1-contact, one alpha 1 beta 2-contact, one heme contact, and two 2,3-DPG-binding sites.
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Max-Planck-Institut für Biochemie, Martinsried.
Rodewald
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Braunitzer
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002335:Carnivora / Q000097:blood*; D006454:Hemoglobins / Q000032:analysis*; D006801:Humans; D008969:Molecular Sequence Data; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000378:metabolism
D000596:Amino Acids; D006454:Hemoglobins; D014357:Trypsin