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

Olianas, A., Meloni, C., Messana, I., Sanna, M. T., Castagnola, M., Manconi, B., Salvadori, S., Giardina, B., Pellegrini, M., Striped mullet (Mugil cephal) hemoglobin system: multiplicity and functional properties, <<JOURNAL OF COMPARATIVE PHYSIOLOGY. B, BIOCHEMICAL, SYSTEMIC, AND ENVIRONMENTAL PHYSIOLOGY>>, 2011; (Febbraio): 187-197 [http://hdl.handle.net/10807/3347]

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

Olianas, Alessandra;Messana, Irene;Sanna, Maria Teresa;Castagnola, Massimo;Manconi, Barbara;Giardina, Bruno;
2011

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
Inglese
Olianas, A., Meloni, C., Messana, I., Sanna, M. T., Castagnola, M., Manconi, B., Salvadori, S., Giardina, B., Pellegrini, M., Striped mullet (Mugil cephal) hemoglobin system: multiplicity and functional properties, <<JOURNAL OF COMPARATIVE PHYSIOLOGY. B, BIOCHEMICAL, SYSTEMIC, AND ENVIRONMENTAL PHYSIOLOGY>>, 2011; (Febbraio): 187-197 [http://hdl.handle.net/10807/3347]
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/10807/3347
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