Carnivora: the primary structure of the hemoglobin from the silver fox (Vulpes vulpes var., Canidae).
The primary structure determination of the hemoglobin alpha- and beta-chains from the silver fox (Vulpes vulpes var., Canidae) is described. The separation of the chains could be achieved directly from the hemoglobin by RP-HPLC as well as by column chromatography of the globin using carboxymethyl-cellulose. Following 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 peptides could be aligned by homology with human and other Carnivora hemoglobins. Compared to human hemoglobin the alpha- and beta-chains of the silver fox exhibit 24 and 13 amino-acid exchanges, respectively. They differ by one alpha- and two beta-chain replacements from the domestic dog and the coyote. The substitutions affecting contact positions are discussed.
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Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
Braunitzer
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002849:Chromatography, Gas; D002853:Chromatography, Liquid; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000737:chemistry; D005589:Foxes / Q000097:blood*; D005914:Globins / Q000032:analysis; D006454:Hemoglobins / Q000032:analysis*; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification; D014357:Trypsin
D000596:Amino Acids; D006454:Hemoglobins; D010455:Peptides; D005914:Globins; D014357:Trypsin