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Biol Chem Hoppe Seyler. 1989 May;370(5):417-23.

Carnivora: primary structure of the hemoglobin from the spotted hyena (Crocuta crocuta, Hyenidae).

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1
Max-Planck-Institut für Biochemie, Martinsried.

Abstract

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.

PMID:
2742752
DOI:
10.1515/bchm3.1989.370.1.417
[Indexed for MEDLINE]

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