Biochemical characterization of hemoglobins from Caspian Sea sturgeons (Acipenser persicus and Acipenser stellatus).
Identifieur interne : 000393 ( Ncbi/Merge ); précédent : 000392; suivant : 000394Biochemical characterization of hemoglobins from Caspian Sea sturgeons (Acipenser persicus and Acipenser stellatus).
Auteurs : Shohreh Ariaeenejad [Iran] ; Mehran Habibi-Rezaei ; Shahla Jamili ; Mohammad Reza Fatemi ; Najmeh Poursasan ; Faizan Ahmad ; Nader Sheibani ; Kaveh Kavousi ; Ali A. Moosavi-MovahediSource :
- Cell biochemistry and biophysics [ 1559-0283 ] ; 2012.
English descriptors
- KwdEn :
- Animals, Calorimetry, Differential Scanning, Circular Dichroism, Electrophoresis, Cellulose Acetate, Electrophoresis, Polyacrylamide Gel, Fishes (blood), Hemoglobins (analysis), Hemoglobins (chemistry), Hemoglobins (isolation & purification), Humans, Isoelectric Focusing, Oceans and Seas, Oxygen (chemistry), Protein Structure, Secondary, Species Specificity.
- MESH :
- chemical , analysis : Hemoglobins.
- blood : Fishes.
- chemical , chemistry : Hemoglobins, Oxygen.
- chemical , isolation & purification : Hemoglobins.
- Animals, Calorimetry, Differential Scanning, Circular Dichroism, Electrophoresis, Cellulose Acetate, Electrophoresis, Polyacrylamide Gel, Humans, Isoelectric Focusing, Oceans and Seas, Protein Structure, Secondary, Species Specificity.
Abstract
Hemoglobin (Hb) variability is a commonly used index of phylogenetic differentiation and molecular adaptation in fish enabling them to adapt to different ecological conditions. In this study, the characteristics of Hbs from two Sturgeon species of the Southern Caspian Sea Basin were investigated. After extraction and separation of hemoglobin from whole blood, the polyacrylamide gel electrophoresis (SDS-PAGE), cellulose acetate electrophoresis, and isoelectric focusing (IEF) were used to confirm Hb variabilities in these fishes. We showed that although both species have variable Hbs with different isoelectric points, their dominant Hbs can be identified. Ion exchange on CM-cellulose chromatography was used for purification of the dominant Hbs from these fishes. The accuracy of the methods was confirmed by IEF and SDS-PAGE. Spectral studies using fluorescence spectrophotometery indicated that although the Hbs from these fishes had similar properties they exhibited clear differences with human Hb. A comparative study of Hbs alpha-helix secondary substructures was performed by circular dichroism spectropolarimetry (CD) analysis. UV-vis spectrophotometery was also utilized to measure oxygen affinity of Hbs by sodium dithionite. Oxygen affinities of these Hbs were compared using Hb-oxygen dissociation curves. Together, these results demonstrate a significant relationship between oxygen affinity of fish hemoglobins and environmental partial pressure of oxygen.
DOI: 10.1007/s12013-011-9261-x
PubMed: 21833671
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Moosavi-Movahedi</name></author></analytic><series><title level="j">Cell biochemistry and biophysics</title><idno type="eISSN">1559-0283</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Calorimetry, Differential Scanning</term><term>Circular Dichroism</term><term>Electrophoresis, Cellulose Acetate</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Fishes (blood)</term><term>Hemoglobins (analysis)</term><term>Hemoglobins (chemistry)</term><term>Hemoglobins (isolation & purification)</term><term>Humans</term><term>Isoelectric Focusing</term><term>Oceans and Seas</term><term>Oxygen (chemistry)</term><term>Protein Structure, Secondary</term><term>Species Specificity</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Hemoglobins</term></keywords><keywords scheme="MESH" qualifier="blood" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemoglobins</term><term>Oxygen</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Hemoglobins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Calorimetry, Differential Scanning</term><term>Circular Dichroism</term><term>Electrophoresis, Cellulose Acetate</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Humans</term><term>Isoelectric Focusing</term><term>Oceans and Seas</term><term>Protein Structure, Secondary</term><term>Species Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Hemoglobin (Hb) variability is a commonly used index of phylogenetic differentiation and molecular adaptation in fish enabling them to adapt to different ecological conditions. In this study, the characteristics of Hbs from two Sturgeon species of the Southern Caspian Sea Basin were investigated. After extraction and separation of hemoglobin from whole blood, the polyacrylamide gel electrophoresis (SDS-PAGE), cellulose acetate electrophoresis, and isoelectric focusing (IEF) were used to confirm Hb variabilities in these fishes. We showed that although both species have variable Hbs with different isoelectric points, their dominant Hbs can be identified. Ion exchange on CM-cellulose chromatography was used for purification of the dominant Hbs from these fishes. The accuracy of the methods was confirmed by IEF and SDS-PAGE. Spectral studies using fluorescence spectrophotometery indicated that although the Hbs from these fishes had similar properties they exhibited clear differences with human Hb. A comparative study of Hbs alpha-helix secondary substructures was performed by circular dichroism spectropolarimetry (CD) analysis. UV-vis spectrophotometery was also utilized to measure oxygen affinity of Hbs by sodium dithionite. Oxygen affinities of these Hbs were compared using Hb-oxygen dissociation curves. Together, these results demonstrate a significant relationship between oxygen affinity of fish hemoglobins and environmental partial pressure of oxygen.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21833671</PMID><DateCreated><Year>2012</Year><Month>01</Month><Day>11</Day></DateCreated><DateCompleted><Year>2012</Year><Month>05</Month><Day>04</Day></DateCompleted><DateRevised><Year>2016</Year><Month>12</Month><Day>29</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1559-0283</ISSN><JournalIssue CitedMedium="Internet"><Volume>62</Volume><Issue>1</Issue><PubDate><Year>2012</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Cell biochemistry and biophysics</Title><ISOAbbreviation>Cell Biochem. 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Ion exchange on CM-cellulose chromatography was used for purification of the dominant Hbs from these fishes. The accuracy of the methods was confirmed by IEF and SDS-PAGE. Spectral studies using fluorescence spectrophotometery indicated that although the Hbs from these fishes had similar properties they exhibited clear differences with human Hb. A comparative study of Hbs alpha-helix secondary substructures was performed by circular dichroism spectropolarimetry (CD) analysis. UV-vis spectrophotometery was also utilized to measure oxygen affinity of Hbs by sodium dithionite. Oxygen affinities of these Hbs were compared using Hb-oxygen dissociation curves. Together, these results demonstrate a significant relationship between oxygen affinity of fish hemoglobins and environmental partial pressure of oxygen.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ariaeenejad</LastName><ForeName>Shohreh</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Marine Biology, Faculty of Marine Science and Technology, Science and Research Branch, Islamic Azad University (IAU), Tehran, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Habibi-Rezaei</LastName><ForeName>Mehran</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Jamili</LastName><ForeName>Shahla</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Fatemi</LastName><ForeName>Mohammad Reza</ForeName><Initials>MR</Initials></Author><Author ValidYN="Y"><LastName>Poursasan</LastName><ForeName>Najmeh</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Ahmad</LastName><ForeName>Faizan</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Sheibani</LastName><ForeName>Nader</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Kavousi</LastName><ForeName>Kaveh</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Moosavi-Movahedi</LastName><ForeName>Ali A</ForeName><Initials>AA</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 EY018179</GrantID><Acronym>EY</Acronym><Agency>NEI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Cell Biochem 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Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="N">Fishes</DescriptorName><QualifierName UI="Q000097" MajorTopicYN="Y">blood</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006454" MajorTopicYN="N">Hemoglobins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007525" MajorTopicYN="N">Isoelectric Focusing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009792" MajorTopicYN="N">Oceans and Seas</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013045" MajorTopicYN="N">Species Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>8</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>8</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>5</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21833671</ArticleId><ArticleId IdType="doi">10.1007/s12013-011-9261-x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Iran</li></country></list><tree><noCountry><name sortKey="Ahmad, Faizan" sort="Ahmad, Faizan" uniqKey="Ahmad F" first="Faizan" last="Ahmad">Faizan Ahmad</name><name sortKey="Fatemi, Mohammad Reza" sort="Fatemi, Mohammad Reza" uniqKey="Fatemi M" first="Mohammad Reza" last="Fatemi">Mohammad Reza Fatemi</name><name sortKey="Habibi Rezaei, Mehran" sort="Habibi Rezaei, Mehran" uniqKey="Habibi Rezaei M" first="Mehran" last="Habibi-Rezaei">Mehran Habibi-Rezaei</name><name sortKey="Jamili, Shahla" sort="Jamili, Shahla" uniqKey="Jamili S" first="Shahla" last="Jamili">Shahla Jamili</name><name sortKey="Kavousi, Kaveh" sort="Kavousi, Kaveh" uniqKey="Kavousi K" first="Kaveh" last="Kavousi">Kaveh Kavousi</name><name sortKey="Moosavi Movahedi, Ali A" sort="Moosavi Movahedi, Ali A" uniqKey="Moosavi Movahedi A" first="Ali A" last="Moosavi-Movahedi">Ali A. Moosavi-Movahedi</name><name sortKey="Poursasan, Najmeh" sort="Poursasan, Najmeh" uniqKey="Poursasan N" first="Najmeh" last="Poursasan">Najmeh Poursasan</name><name sortKey="Sheibani, Nader" sort="Sheibani, Nader" uniqKey="Sheibani N" first="Nader" last="Sheibani">Nader Sheibani</name></noCountry><country name="Iran"><noRegion><name sortKey="Ariaeenejad, Shohreh" sort="Ariaeenejad, Shohreh" uniqKey="Ariaeenejad S" first="Shohreh" last="Ariaeenejad">Shohreh Ariaeenejad</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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