The oxygen-binding modulation of hemocyanin from the Southern spiny lobster Palinurus gilchristi.
Identifieur interne : 002763 ( Main/Exploration ); précédent : 002762; suivant : 002764The oxygen-binding modulation of hemocyanin from the Southern spiny lobster Palinurus gilchristi.
Auteurs : Alessandra Olianas [Italie] ; Barbara Manconi ; Daniela Masia ; Maria T. Sanna ; Massimo Castagnola ; Susanna Salvadori ; Irene Messana ; Bruno Giardina ; Mariagiuseppina PellegriniSource :
- Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology [ 1432-136X ] ; 2009.
Descripteurs français
- KwdFr :
- Acide lactique (métabolisme), Acide urique (métabolisme), Animaux, Calcium (métabolisme), Concentration en ions d'hydrogène, Oxygène (métabolisme), Palinuridae (métabolisme), Sites de fixation (génétique), Sous-unités de protéines (métabolisme), Spectrophotométrie, Électrophorèse sur gel de polyacrylamide.
- MESH :
English descriptors
- KwdEn :
- Animals, Binding Sites (genetics), Calcium (metabolism), Electrophoresis, Polyacrylamide Gel, Hemocyanins (genetics), Hemocyanins (metabolism), Hydrogen-Ion Concentration, Lactic Acid (metabolism), Oxygen (metabolism), Palinuridae (metabolism), Protein Subunits (metabolism), Spectrophotometry, Uric Acid (metabolism).
- MESH :
- chemical , genetics : Hemocyanins.
- chemical , metabolism : Calcium, Hemocyanins, Lactic Acid, Oxygen, Protein Subunits, Uric Acid.
- genetics : Binding Sites.
- metabolism : Palinuridae.
- Animals, Electrophoresis, Polyacrylamide Gel, Hydrogen-Ion Concentration, Spectrophotometry.
Abstract
Arthropod hemocyanins transport and store oxygen and are composed of six subunits, or multiples thereof depending on the species. Palinurus gilchristi hemocyanin is found only as 1 x 6-mers, as normally occurs in spiny lobsters. An alkaline pH and removal of calcium ions induce a wholly reversible dissociation into monomers. The oxygen-binding properties of 1 x 6-meric hemocyanin from P. gilchristi were investigated with respect to pH and modulating effect exerted by calcium, lactate and urate. The oxygen affinity was highly affected by pH in the presence of calcium ions, while in its absence the Bohr coefficient became 60% lower. The protein is insensitive to lactate, but affected by urate which markedly increased hemocyanin-oxygen affinity, acting as the physiological major positive effector. Calcium ions decrease oxygen affinity at low concentration range (0-1 mM), while as concentration becomes higher than 100 mM, the oxygen affinity increases, indicating the presence of two independent types of calcium-binding sites with high and low affinity, respectively. The previous hypothesis, that the presence of high-affinity binding sites in addition to low affinity ones could be a characteristic feature of Palinuran hemocyanins, has been tested by analyzing, with respect to calcium-hemocyanin interaction, three other species belonging to Palinura.
DOI: 10.1007/s00360-008-0302-8
PubMed: 18807050
Affiliations:
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Le document en format XML
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Sanna</name></author><author><name sortKey="Castagnola, Massimo" sort="Castagnola, Massimo" uniqKey="Castagnola M" first="Massimo" last="Castagnola">Massimo Castagnola</name></author><author><name sortKey="Salvadori, Susanna" sort="Salvadori, Susanna" uniqKey="Salvadori S" first="Susanna" last="Salvadori">Susanna Salvadori</name></author><author><name sortKey="Messana, Irene" sort="Messana, Irene" uniqKey="Messana I" first="Irene" last="Messana">Irene Messana</name></author><author><name sortKey="Giardina, Bruno" sort="Giardina, Bruno" uniqKey="Giardina B" first="Bruno" last="Giardina">Bruno Giardina</name></author><author><name sortKey="Pellegrini, Mariagiuseppina" sort="Pellegrini, Mariagiuseppina" uniqKey="Pellegrini M" first="Mariagiuseppina" last="Pellegrini">Mariagiuseppina Pellegrini</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:18807050</idno><idno type="pmid">18807050</idno><idno type="doi">10.1007/s00360-008-0302-8</idno><idno type="wicri:Area/PubMed/Corpus">002077</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002077</idno><idno type="wicri:Area/PubMed/Curation">002077</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002077</idno><idno type="wicri:Area/PubMed/Checkpoint">001E77</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001E77</idno><idno type="wicri:Area/Ncbi/Merge">000632</idno><idno type="wicri:Area/Ncbi/Curation">000632</idno><idno type="wicri:Area/Ncbi/Checkpoint">000632</idno><idno type="wicri:Area/Main/Merge">002788</idno><idno type="wicri:Area/Main/Curation">002763</idno><idno type="wicri:Area/Main/Exploration">002763</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The oxygen-binding modulation of hemocyanin from the Southern spiny lobster Palinurus gilchristi.</title><author><name sortKey="Olianas, Alessandra" sort="Olianas, Alessandra" uniqKey="Olianas A" first="Alessandra" last="Olianas">Alessandra Olianas</name><affiliation wicri:level="1"><nlm:affiliation>Department of Sciences Applied to Biosystems, University of Cagliari, Cittadella Universitaria, 09042 Monserrato (CA), Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Sciences Applied to Biosystems, University of Cagliari, Cittadella Universitaria, 09042 Monserrato (CA)</wicri:regionArea><wicri:noRegion>09042 Monserrato (CA)</wicri:noRegion></affiliation></author><author><name sortKey="Manconi, Barbara" sort="Manconi, Barbara" uniqKey="Manconi B" first="Barbara" last="Manconi">Barbara Manconi</name></author><author><name sortKey="Masia, Daniela" sort="Masia, Daniela" uniqKey="Masia D" first="Daniela" last="Masia">Daniela Masia</name></author><author><name sortKey="Sanna, Maria T" sort="Sanna, Maria T" uniqKey="Sanna M" first="Maria T" last="Sanna">Maria T. 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Palinurus gilchristi hemocyanin is found only as 1 x 6-mers, as normally occurs in spiny lobsters. An alkaline pH and removal of calcium ions induce a wholly reversible dissociation into monomers. The oxygen-binding properties of 1 x 6-meric hemocyanin from P. gilchristi were investigated with respect to pH and modulating effect exerted by calcium, lactate and urate. The oxygen affinity was highly affected by pH in the presence of calcium ions, while in its absence the Bohr coefficient became 60% lower. The protein is insensitive to lactate, but affected by urate which markedly increased hemocyanin-oxygen affinity, acting as the physiological major positive effector. Calcium ions decrease oxygen affinity at low concentration range (0-1 mM), while as concentration becomes higher than 100 mM, the oxygen affinity increases, indicating the presence of two independent types of calcium-binding sites with high and low affinity, respectively. The previous hypothesis, that the presence of high-affinity binding sites in addition to low affinity ones could be a characteristic feature of Palinuran hemocyanins, has been tested by analyzing, with respect to calcium-hemocyanin interaction, three other species belonging to Palinura.</div></front></TEI><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Castagnola, Massimo" sort="Castagnola, Massimo" uniqKey="Castagnola M" first="Massimo" last="Castagnola">Massimo Castagnola</name><name sortKey="Giardina, Bruno" sort="Giardina, Bruno" uniqKey="Giardina B" first="Bruno" last="Giardina">Bruno Giardina</name><name sortKey="Manconi, Barbara" sort="Manconi, Barbara" uniqKey="Manconi B" first="Barbara" last="Manconi">Barbara Manconi</name><name sortKey="Masia, Daniela" sort="Masia, Daniela" uniqKey="Masia D" first="Daniela" last="Masia">Daniela Masia</name><name sortKey="Messana, Irene" sort="Messana, Irene" uniqKey="Messana I" first="Irene" last="Messana">Irene Messana</name><name sortKey="Pellegrini, Mariagiuseppina" sort="Pellegrini, Mariagiuseppina" uniqKey="Pellegrini M" first="Mariagiuseppina" last="Pellegrini">Mariagiuseppina Pellegrini</name><name sortKey="Salvadori, Susanna" sort="Salvadori, Susanna" uniqKey="Salvadori S" first="Susanna" last="Salvadori">Susanna Salvadori</name><name sortKey="Sanna, Maria T" sort="Sanna, Maria T" uniqKey="Sanna M" first="Maria T" last="Sanna">Maria T. Sanna</name></noCountry><country name="Italie"><noRegion><name sortKey="Olianas, Alessandra" sort="Olianas, Alessandra" uniqKey="Olianas A" first="Alessandra" last="Olianas">Alessandra Olianas</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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