Striped mullet (Mugil cephal) hemoglobin system: multiplicity and functional properties

Alessandra Olianas, Irene Messana, Maria Teresa Sanna, Massimo Castagnola, Barbara Manconi, Bruno Giardina, Claudia Meloni, Susanna Salvadori, Mariagiuseppina Pellegrini

Risultato della ricerca: Contributo in rivistaArticolo in rivista

Abstract

The most frequent (90%) phenotype of the hemoglobin system of M. cephalus presented two major hemoglobins, the more anodal HbI accounting for approximately 70% of the total. The two hemoglobin components separated by ion-exchange chromatography were analyzed by reverse-phase HPLC and electrospray ionization-mass spectrometry which revealed a more complex pattern: HbI consists in four different globins, two b(namedb1andb3) and two co-eluting achains(a1 and a2); HbII consists in three globins, one bchain(namedb2) and the same a1 and a2 present in HbI. Theoxygen-binding properties of both hemoglobin components purified by DEAE cellulose were almost identical to those of the hemolysate: stripped hemoglobins howed a large Bohr effect which was enhanced by chloride ions and, a ta larger extent, by organic phosphates which, at acidic pH values gave rise to the Root effect. A series of oxygen-binding experiments at increasing GTP concentrations was carried out in order to compare GTP-binding activities in the absence and presence of physiological amount sofchloride
Lingua originaleEnglish
pagine (da-a)187-197
Numero di pagine11
RivistaJOURNAL OF COMPARATIVE PHYSIOLOGY. B, BIOCHEMICAL, SYSTEMIC, AND ENVIRONMENTAL PHYSIOLOGY
Stato di pubblicazionePubblicato - 2011

Keywords

  • Bohr effect
  • Electrospray ionization-mass spectrometry
  • Hemoglobin
  • Mugil cephalus

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