Carnivora: primary structure of the hemoglobins from ratel (Mellivora capensis).
The erythrocytes of adult ratel contain two hemoglobin components, with two alpha- and one beta-chains. In this paper, their complete amino acid sequences are presented. The two alpha-chains differ in one residue at position 34 (Ala----Val) only. The primary structure of the chains was determined by sequencing the N-terminal regions (45 steps) and the tryptic peptides after their isolation from the digests by reversed-phase high-performance liquid chromatography. The alignment of these peptides was deduced from homology with other carnivora globins. The alpha-chains show 21 and the beta-chains 11 exchanges compared with human globin chains. In the alpha-chains, one heme- and two alpha 1/beta 1 contacts are exchanged. In the beta-chains there are three exchanges which involve one alpha 1/beta 1-, one alpha 1/beta 2- and one heme-contact. Between the ratel hemoglobin and those of carnivora a high degree of homology was found.
Rodewald
K
K
Max-Planck-Institut für Biochemie, Martinsried bei München.
Braunitzer
G
G
Göltenboth
R
R
D000595:Amino Acid Sequence; D000818:Animals; D002335:Carnivora / Q000097:blood*; D002851:Chromatography, High Pressure Liquid; D006454:Hemoglobins / Q000302:isolation & purification; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D014357:Trypsin
D006454:Hemoglobins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D014357:Trypsin