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Functional characterization of the single hemoglobin of the migratory bird Ciconia ciconia.

Functional characterization of the single hemoglobin of the migratory bird Ciconia ciconia. Research Abstract Details 

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  • Functional characterization of the single hemoglobin of the migratory bird Ciconia ciconia. Abstract Text:

    barbara manconiBarbara Manconi,alessandra olianasAlessandra Olianas,maria t sannaMaria T Sanna,irene messanaIrene Messana,loredana demurtasLoredana Demurtas,massimo castagnolaMassimo Castagnola,bruno giardinaBruno Giardina,mariagiuseppina pellegriniMariagiuseppina Pellegrini,barbara manconiBarbara Manconi,alessandra olianasAlessandra Olianas,maria t sannaMaria T Sanna,irene messanaIrene Messana,loredana demurtasLoredana Demurtas,massimo castagnolaMassimo Castagnola,bruno giardinaBruno Giardina,mariagiuseppina pellegriniMariagiuseppina Pellegrini,

    Hemolysate from white stork displayed a single hemoglobin component, thus resulting into two bands and two globin peaks in dissociating PAGE and reversed phase-HPLC, respectively. Stripped hemoglobin showed an oxygen affinity higher than that of human HbA, a small Bohr effect, and a cooperative oxygen binding. A small decrease of oxygen affinity, of the same extent in all the pH range examined, was observed by addition of chloride, thus indicating an unusual chloride-independent Bohr effect (DeltalogP50/Deltalog pH=-0.24). Saturating amounts of inositol hexakisphosphate, largely decreased hemoglobin-oxygen affinity (DeltalogP(50)=1.17 at pH 7.0), and increased the extent of its Bohr effect (DeltalogP50/DeltalogpH=-0.45). The phosphate binding curve allowed to measure a very high overall binding constant (K=1.18 x 10(5) M(-1)). The effect of temperature on the oxygen affinity was measured, and the enthalpy change of oxygenation resulted almost independent on pH. Structural-functional relationships are discussed by considering some amino acid residues situated at alpha1/beta1 and alpha1/beta2 interfaces, such as alpha38 and alpha89 positions. The presence of only one hemoglobin component, a rare event among birds, and its functional properties have been related to the physiological oxygen requirements of this soaring migrant bird and to its technique of flight during migration.

    Functional characterization of the single hemoglobin of the migratory bird Ciconia ciconia. Publishing Authors By Initials

    b manconiB Manconi,a olianasA Olianas,mt sannaMT Sanna,i messanaI Messana,l demurtasL Demurtas,m castagnolaM Castagnola,b giardinaB Giardina,m pellegriniM Pellegrini,b manconiB Manconi,a olianasA Olianas,mt sannaMT Sanna,i messanaI Messana,l demurtasL Demurtas,m castagnolaM Castagnola,b giardinaB Giardina,m pellegriniM Pellegrini,

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    Functional characterization of the single hemoglobin of the migratory bird Ciconia ciconia. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Comparative biochemistry and physiology. Part B, B

    VOLUME: 147

    Page Numbers: 242-9

    Journal Abbreviation:

    ISSN: 1096-4959

    DAY: 1

    MONTH: 02

    YEAR: 2007

    Functional characterization of the single hemoglobin of the migratory bird Ciconia ciconia. Information

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    LANGUAGE: eng

    NlmUniqueID: 9516061

    Functional characterization of the single hemoglobin of the migratory bird Ciconia ciconia. Keywords Mesh Terms:

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    Grant and Affiliation Information for Functional characterization of the single hemoglobin of the migratory bird Ciconia ciconia.

    AFFILIATION: Dipartimento di Scienze Applicate ai Biosistemi, Università di Cagliari, Cittadella Universitaria, I-09042 Monserrato (CA) Italy.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: Comp Biochem Physiol B Biochem

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