Carnivora: the primary structure of the alpha-chains of ferret (Mustela putorius furo, Mustelidae) hemoglobins.
Ferret erythrocytes contain two hemoglobins differing only by their alpha-chains. The primary structure of the common beta-chain has been previously described; the complete sequence of the two alpha-chains are reported in this paper. The globin chains were separated by ion-exchange chromatography; the alpha-chains (42 steps), their tryptic peptides as well as the prolyl-peptides were subjected to automatic liquid- and gas-phase Edman degradation. The two alpha-chains are very similar, differing at only one position (Asp15----Gly15). Comparison with human hemoglobin alpha-chain shows 16 and 17 exchanges, for alpha 1 and alpha II chains, respectively; two substitutions involve alpha 1/beta 1 contacts and one the heme contacts. A high degree of homology was noted when the alpha-chains were compared to the corresponding chains of other representatives of the Carnivora order.
Hombrados
I
I
Laboratoire de Biochimie Médicale, Université de Bordeaux II.
Vidal
Y
Y
Rodewald
K
K
Braunitzer
G
G
Neuzil
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002335:Carnivora / Q000097:blood*; D005289:Ferrets / Q000097:blood*; D006454:Hemoglobins / Q000032:analysis*; D006801:Humans; D008969:Molecular Sequence Data
D006454:Hemoglobins