The primary structure of the hemoglobin from the aardwolf (Proteles cristatus, Hyaenidae).
The hemoglobin of the aardwolf (Proteles cristatus) contains only one component. In this paper, we are presenting its primary structure. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid and gas-phase Edman degradation of the chains and their tryptic peptides. The alpha- as well as the beta-chains show 20 exchanges compared with the corresponding human chains. The difference to the masked palm civet (Paguma larvata) and the spotted hyaena (Crocuta crocuta) is marked by 16 and 4 replacements in the alpha-chains and by 10 and 1 in the beta-chains, thus supporting the hyaenid character of the aardwolf. The exchanges at contact positions are shared by other carnivoran hemoglobins.
Stoeva
S
S
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei Munchen.
Kleinschmidt
T
T
Braunitzer
G
G
Scheil
H G
HG
D000595:Amino Acid Sequence; D000818:Animals; D002335:Carnivora / Q000235:genetics*; D002851:Chromatography, High Pressure Liquid; D000882:Haplorhini / Q000235:genetics; D006441:Hemoglobin A / Q000235:genetics; D006454:Hemoglobins / Q000235:genetics*; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010802:Phylogeny; D012689:Sequence Homology, Nucleic Acid
D006454:Hemoglobins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D006441:Hemoglobin A