The oxygen-binding modulation of hemocyanin from the Southern spiny lobster Palinurus gilchristi.
Identifieur interne : 000632 ( Ncbi/Merge ); précédent : 000631; suivant : 000633The 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
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002077
- to stream PubMed, to step Curation: 002077
- to stream PubMed, to step Checkpoint: 001E77
Links to Exploration step
pubmed:18807050Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><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. 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></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. 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></analytic><series><title level="j">Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology</title><idno type="eISSN">1432-136X</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Binding Sites (genetics)</term><term>Calcium (metabolism)</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Hemocyanins (genetics)</term><term>Hemocyanins (metabolism)</term><term>Hydrogen-Ion Concentration</term><term>Lactic Acid (metabolism)</term><term>Oxygen (metabolism)</term><term>Palinuridae (metabolism)</term><term>Protein Subunits (metabolism)</term><term>Spectrophotometry</term><term>Uric Acid (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide lactique (métabolisme)</term><term>Acide urique (métabolisme)</term><term>Animaux</term><term>Calcium (métabolisme)</term><term>Concentration en ions d'hydrogène</term><term>Oxygène (métabolisme)</term><term>Palinuridae (métabolisme)</term><term>Sites de fixation (génétique)</term><term>Sous-unités de protéines (métabolisme)</term><term>Spectrophotométrie</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hemocyanins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term><term>Hemocyanins</term><term>Lactic Acid</term><term>Oxygen</term><term>Protein Subunits</term><term>Uric Acid</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Binding Sites</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Sites de fixation</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Palinuridae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide lactique</term><term>Acide urique</term><term>Calcium</term><term>Oxygène</term><term>Palinuridae</term><term>Sous-unités de protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Hydrogen-Ion Concentration</term><term>Spectrophotometry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Concentration en ions d'hydrogène</term><term>Spectrophotométrie</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18807050</PMID><DateCompleted><Year>2009</Year><Month>06</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-136X</ISSN><JournalIssue CitedMedium="Internet"><Volume>179</Volume><Issue>2</Issue><PubDate><Year>2009</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology</Title><ISOAbbreviation>J. Comp. Physiol. B, Biochem. Syst. Environ. Physiol.</ISOAbbreviation></Journal><ArticleTitle>The oxygen-binding modulation of hemocyanin from the Southern spiny lobster Palinurus gilchristi.</ArticleTitle><Pagination><MedlinePgn>193-203</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00360-008-0302-8</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Olianas</LastName><ForeName>Alessandra</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Sciences Applied to Biosystems, University of Cagliari, Cittadella Universitaria, 09042 Monserrato (CA), Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Manconi</LastName><ForeName>Barbara</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Masia</LastName><ForeName>Daniela</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Sanna</LastName><ForeName>Maria T</ForeName><Initials>MT</Initials></Author><Author ValidYN="Y"><LastName>Castagnola</LastName><ForeName>Massimo</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Salvadori</LastName><ForeName>Susanna</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Messana</LastName><ForeName>Irene</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Giardina</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Pellegrini</LastName><ForeName>Mariagiuseppina</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>09</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>J Comp Physiol B</MedlineTA><NlmUniqueID>8413200</NlmUniqueID><ISSNLinking>0174-1578</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance></Chemical><Chemical><RegistryNumber>268B43MJ25</RegistryNumber><NameOfSubstance UI="D014527">Uric Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>33X04XA5AT</RegistryNumber><NameOfSubstance UI="D019344">Lactic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>9013-72-3</RegistryNumber><NameOfSubstance UI="D006433">Hemocyanins</NameOfSubstance></Chemical><Chemical><RegistryNumber>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006433" MajorTopicYN="N">Hemocyanins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019344" MajorTopicYN="N">Lactic Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D033521" MajorTopicYN="N">Palinuridae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014527" MajorTopicYN="N">Uric Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2008</Year><Month>03</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2008</Year><Month>09</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2008</Year><Month>07</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>9</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>6</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>9</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18807050</ArticleId><ArticleId IdType="doi">10.1007/s00360-008-0302-8</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Q Rev Biophys. 1982 Feb;15(1):1-129</Citation><ArticleIdList><ArticleId IdType="pubmed">7048392</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1970 Aug 15;227(5259):680-5</Citation><ArticleIdList><ArticleId IdType="pubmed">5432063</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1966 Feb 25;151(3713):1005-7</Citation><ArticleIdList><ArticleId IdType="pubmed">5907286</ArticleId></ArticleIdList></Reference><Reference><Citation>J Comp Physiol B. 2005 Aug;175(6):405-11</Citation><ArticleIdList><ArticleId IdType="pubmed">16010551</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1983 Sep 27;22(20):4713-23</Citation><ArticleIdList><ArticleId IdType="pubmed">6626526</ArticleId></ArticleIdList></Reference><Reference><Citation>Biophys Chem. 2001 May 18;90(3):279-99</Citation><ArticleIdList><ArticleId IdType="pubmed">11407645</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1982 Jun 15;125(1):103-8</Citation><ArticleIdList><ArticleId IdType="pubmed">7106115</ArticleId></ArticleIdList></Reference><Reference><Citation>Respir Physiol. 1975 Jul;24(2):173-89</Citation><ArticleIdList><ArticleId IdType="pubmed">241104</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1976 Dec 14;15(25):5527-33</Citation><ArticleIdList><ArticleId IdType="pubmed">999826</ArticleId></ArticleIdList></Reference><Reference><Citation>Comp Biochem Physiol A Mol Integr Physiol. 2000 Oct;127(2):147-54</Citation><ArticleIdList><ArticleId IdType="pubmed">11064282</ArticleId></ArticleIdList></Reference><Reference><Citation>J Exp Biol. 2001 Mar;204(Pt 5):1033-8</Citation><ArticleIdList><ArticleId IdType="pubmed">11171426</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biochem. 2006 Jun;139(6):957-66</Citation><ArticleIdList><ArticleId IdType="pubmed">16788046</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS J. 2005 Apr;272(8):2060-75</Citation><ArticleIdList><ArticleId IdType="pubmed">15819896</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1984 Feb 28;23(5):872-8</Citation><ArticleIdList><ArticleId IdType="pubmed">25856833</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1988 Apr 15;173(2):423-30</Citation><ArticleIdList><ArticleId IdType="pubmed">3360019</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1986 Jan 2;154(1):49-55</Citation><ArticleIdList><ArticleId IdType="pubmed">3943525</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1981;76:417-27</Citation><ArticleIdList><ArticleId IdType="pubmed">7329266</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2000 Sep 5;39(35):10806-11</Citation><ArticleIdList><ArticleId IdType="pubmed">10978166</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1979 Dec 25;18(26):5849-54</Citation><ArticleIdList><ArticleId IdType="pubmed">42435</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1972 Dec 14;72(1):163-97</Citation><ArticleIdList><ArticleId IdType="pubmed">4648112</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1988 Mar 22;27(6):1995-2001</Citation><ArticleIdList><ArticleId IdType="pubmed">2837279</ArticleId></ArticleIdList></Reference><Reference><Citation>Respir Physiol. 1989 Sep;77(3):323-36</Citation><ArticleIdList><ArticleId IdType="pubmed">2781169</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2003 Jan 3;325(1):99-109</Citation><ArticleIdList><ArticleId IdType="pubmed">12473454</ArticleId></ArticleIdList></Reference><Reference><Citation>Comp Biochem Physiol. 1964 Sep;13:35-46</Citation><ArticleIdList><ArticleId IdType="pubmed">14221829</ArticleId></ArticleIdList></Reference><Reference><Citation>Comp Biochem Physiol B Biochem Mol Biol. 2004 Oct;139(2):261-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15465673</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Evol. 2001 Feb;18(2):184-95</Citation><ArticleIdList><ArticleId IdType="pubmed">11158377</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 2003 Apr 15;371(Pt 2):515-23</Citation><ArticleIdList><ArticleId IdType="pubmed">12466021</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1966 Jun;5(6):1943-51</Citation><ArticleIdList><ArticleId IdType="pubmed">5963436</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1981;76:470-86</Citation><ArticleIdList><ArticleId IdType="pubmed">7329271</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1975 Dec 25;99(4):619-29</Citation><ArticleIdList><ArticleId IdType="pubmed">2785</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1989 Apr 5;206(3):531-46</Citation><ArticleIdList><ArticleId IdType="pubmed">2716060</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Protein Chem. 1995;47:1-81</Citation><ArticleIdList><ArticleId IdType="pubmed">8561049</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 1987 Dec 18;916(3):376-80</Citation><ArticleIdList><ArticleId IdType="pubmed">3689798</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><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)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Ncbi/Merge
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000632 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 000632 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Ncbi
|étape= Merge
|type= RBID
|clé= pubmed:18807050
|texte= The oxygen-binding modulation of hemocyanin from the Southern spiny lobster Palinurus gilchristi.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i -Sk "pubmed:18807050" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |