title: Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi.
abstract: Antarctic fish of the family Nototheniidae usually have a single major hemoglobin (Hb 1), often a second, minor component (Hb 2, about 5% of the total), and traces of another component (Hb C, less than 1%). These are functionally similar Bohr and Root effect hemoglobins. All species of other highly endemic fish families so far investigated also have one single major hemoglobin. The hematological features of the nototheniid Trematomus newnesi are remarkably different. It is the only Antarctic species in which Hb 1 and Hb 2 display only a very weak Bohr effect and no Root effect. Perhaps consequentially, Hb C (the only component showing regulation of oxygen binding by protons and other effectors) is not present in traces but accounts for 20-25% of the total. The primary structure of the three hemoglobins of T. newnesi and of Root effect HbC present in trace amounts in another nototheniid (Pagothenia bernacchii) is discussed in relationship with oxygen binding and in terms of molecular and stereochemical models. The hemoglobin multiplicity, the oxygen binding features of Hb 1 and Hb 2, and the presence of functionally distinct components, thus reveal that the oxygen transport of T. newnesi has unique characteristics.
authors.affiliation: Institute of Protein Biochemistry and Enzymology, Consiglio Nazionale delle Ricerche, Naples, Italy.
authors.forename: R
authors.initials: R
authors.lastname: D'Avino
authors.forename: C
authors.initials: C
authors.lastname: Caruso
authors.forename: M
authors.initials: M
authors.lastname: Tamburrini
authors.forename: M
authors.initials: M
authors.lastname: Romano
authors.forename: B
authors.initials: B
authors.lastname: Rutigliano
authors.forename: P
authors.initials: P
authors.lastname: Polverino de Laureto
authors.forename: L
authors.initials: L
authors.lastname: Camardella
authors.forename: V
authors.initials: V
authors.lastname: Carratore
authors.forename: G
authors.initials: G
authors.lastname: di Prisco
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001110:Arctic Regions; D002852:Chromatography, Ion Exchange; D004588:Electrophoresis, Cellulose Acetate; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes / Q000097:blood*; D005914:Globins / Q000737:chemistry* / Q000302:isolation & purification; D006454:Hemoglobins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010108:Oxyhemoglobins / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D014357:Trypsin
chemical_list: D000596:Amino Acids; D006454:Hemoglobins; D046911:Macromolecular Substances; D010108:Oxyhemoglobins; D010446:Peptide Fragments; D005914:Globins; D014357:Trypsin