Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus (Articolo in rivista)

Type
Label
  • Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.gene.2007.06.002 (literal)
Alternative label
  • Giordano D, Vergara A, Lee HC, Peisach J, Balestrieri M, Mazzarella L, Parisi E, di Prisco G, Verde C. (2007)
    Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus
    in Gene (Amst.)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Giordano D, Vergara A, Lee HC, Peisach J, Balestrieri M, Mazzarella L, Parisi E, di Prisco G, Verde C. (literal)
Pagina inizio
  • 58 (literal)
Pagina fine
  • 68 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 406 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1-2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. CNR, Inst Protein Biochem, I-80131 Naples, Italy 2. Univ Naples Federico 2, Dipartimento Chim, I-80126 Naples, Italy 3. Yeshiva Univ, Albert Einstein Coll Med, Dept Physiol & Biophys, Bronx, NY 10461 USA (literal)
Titolo
  • Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus (literal)
Abstract
  • The importance of the Arctic, in contributing to the knowledge of the overall ensemble of adaptive processes influencing the evolution of marine organisms, calls for investigations on molecular adaptations in Arctic fish. Unlike the vast majority of Antarctic Notothenioidei, several Arctic species display high hemoglobin multiplicity. The blood of four species, the spotted wolffish of the family Anarhichadidae and three Gadidae, contains three functionally distinct major components. Similar to many Antarctic notothenioids, Arctic Liparis tunicatus (suborder Cottoidei, family Liparidae) has one major hemoglobin (Hb 1) accompanied by a minor component (Hb 2). This paper reports the structural and functional characterisation of Hb 1 of L. tunicatus. This hemoglobin shows low oxygen affinity, and pronounced Bohr and Root effects. The amino-acid sequence of the beta chain displays an unusual substitution in NA2 (beta2) at the phosphate-binding site, and the replacement of Val E11 (beta67) with Ile. Similar to some Antarctic fish Hbs, electron paramagnetic resonance spectra reveal the formation of a ferric penta-coordinated species even at physiological pH. The amino-acid sequences have also been used to gain insight into the evolutionary history of globins of polar fish. L. tunicatus globins appear close to the notothenioid clades as predicted by teleostean phylogenies. Close phylogenetic relationships between Cottoidei and Notothenioidei, together with their life style, seem to be the main factor driving the globin-sequence evolution. (literal)
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