title: The primary structure of hemoglobin from reindeer (Rangifer tarandus tarandus) and its functional implications.
abstract: The primary structures of alpha- and beta-chains of hemoglobin from reindeer (Rangifer tarandus tarandus) were determined. Comparison of the reindeer hemoglobin sequence with those of human and bovine hemoglobins showed 50 and 29 substitutions per alpha beta dimer, respectively. The influence of replacements on the modulation of hemoglobin oxygen affinity by heterothopic ligands and temperature, as well as their importance on the structure-function relationships in hemoglobin are discussed.
authors.affiliation: Dipartimento di Biologia, Università di Roma Tor Vergata, Italy.
authors.forename: R
authors.initials: R
authors.lastname: Petruzzelli
authors.forename: D
authors.initials: D
authors.lastname: Barra
authors.forename: F
authors.initials: F
authors.lastname: Bossa
authors.forename: S G
authors.initials: SG
authors.lastname: Condò
authors.forename: O
authors.initials: O
authors.lastname: Brix
authors.forename: M
authors.initials: M
authors.lastname: Nuutinen
authors.forename: B
authors.initials: B
authors.lastname: Giardina
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle / Q000097:blood; D003670:Deer / Q000097:blood; D006454:Hemoglobins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010108:Oxyhemoglobins / Q000378:metabolism; D012053:Reindeer / Q000097:blood*; D012689:Sequence Homology, Nucleic Acid
chemical_list: D006454:Hemoglobins; D010108:Oxyhemoglobins