Denaturation and intermediates study of two sturgeon hemoglobins by n-dodecyl trimethylammonium bromide.
Identifieur interne : 000300 ( Main/Merge ); précédent : 000299; suivant : 000301Denaturation and intermediates study of two sturgeon hemoglobins by n-dodecyl trimethylammonium bromide.
Auteurs : Shohreh Ariaeenejad [Iran] ; Mehran Habibi-Rezaei ; Kaveh Kavousi ; Shahla Jamili ; Mohammad Reza Fatemi ; Jun Hong ; Najmeh Poursasan ; Nader Sheibani ; Ali A. Moosavi-MovahediSource :
- International journal of biological macromolecules [ 1879-0003 ] ; 2013.
English descriptors
- KwdEn :
- Animals, Detergents (chemistry), Dithiothreitol (chemistry), Ecosystem, Fish Proteins (chemistry), Fishes, Hemoglobins (chemistry), Hydrophobic and Hydrophilic Interactions, Oxidation-Reduction, Particle Size, Protein Binding, Protein Denaturation, Protein Stability, Quaternary Ammonium Compounds (chemistry), Reducing Agents (chemistry), Thermodynamics, Titrimetry.
- MESH :
- chemical , chemistry : Detergents, Dithiothreitol, Fish Proteins, Hemoglobins, Quaternary Ammonium Compounds, Reducing Agents.
- Animals, Ecosystem, Fishes, Hydrophobic and Hydrophilic Interactions, Oxidation-Reduction, Particle Size, Protein Binding, Protein Denaturation, Protein Stability, Thermodynamics, Titrimetry.
Abstract
Varieties of hemoglobin (Hb) forms exist in fish, which are usually well adapted to the different ecological conditions or various habitats. In the current study, Hbs from two Sturgeon species of the Southern Caspian Sea Basin were purified and studied upon interaction with n-dodecyl trimethylammonium bromide (DTAB; as a cationic surfactant) by various methods including UV-visible absorption, dynamic light scattering (DLS), and ANS fluorescence spectrophotometry. The chemometric analysis of Hbs was investigated upon interaction with DTAB under titration, using UV-visible absorption spectra. The chemometric resolution techniques were used to determine the number of the components and mole fraction of the oxidized Hbs. These results provided the evidence for the existence of three different molecular components including native (N), intermediate (I) and denatured (D) in sturgeon Hbs. According to the distribution of intermediates, which were broadened in a range of DTAB concentration, the aggregation states, DLS experiments, and thermal stability (T(m) obtained by differential scanning calorimetry (DSC)), the Acipenser stellatus Hb was more stable compared to Acipenser persicus Hb. These results demonstrate a significant relationship between the stability of fish Hbs and the habitat depth requirements.
DOI: 10.1016/j.ijbiomac.2012.10.015
PubMed: 23142155
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Moosavi-Movahedi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23142155</idno><idno type="pmid">23142155</idno><idno type="doi">10.1016/j.ijbiomac.2012.10.015</idno><idno type="wicri:Area/PubMed/Corpus">000274</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000274</idno><idno type="wicri:Area/PubMed/Curation">000274</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000274</idno><idno type="wicri:Area/PubMed/Checkpoint">000274</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000274</idno><idno type="wicri:Area/Ncbi/Merge">000455</idno><idno type="wicri:Area/Ncbi/Curation">000455</idno><idno type="wicri:Area/Ncbi/Checkpoint">000455</idno><idno type="wicri:Area/Main/Merge">000300</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Denaturation and intermediates study of two sturgeon hemoglobins by n-dodecyl trimethylammonium bromide.</title><author><name sortKey="Ariaeenejad, Shohreh" sort="Ariaeenejad, Shohreh" uniqKey="Ariaeenejad S" first="Shohreh" last="Ariaeenejad">Shohreh Ariaeenejad</name><affiliation wicri:level="1"><nlm:affiliation>Department of Marine Biology, Faculty of Marine Science and Technology, Science and Research Branch, Islamic Azad University, Tehran, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Department of Marine Biology, Faculty of Marine Science and Technology, Science and Research Branch, Islamic Azad University, Tehran</wicri:regionArea><wicri:noRegion>Tehran</wicri:noRegion></affiliation></author><author><name sortKey="Habibi Rezaei, Mehran" sort="Habibi Rezaei, Mehran" uniqKey="Habibi Rezaei M" first="Mehran" last="Habibi-Rezaei">Mehran Habibi-Rezaei</name></author><author><name sortKey="Kavousi, Kaveh" sort="Kavousi, Kaveh" uniqKey="Kavousi K" first="Kaveh" last="Kavousi">Kaveh Kavousi</name></author><author><name sortKey="Jamili, Shahla" sort="Jamili, Shahla" uniqKey="Jamili S" first="Shahla" last="Jamili">Shahla Jamili</name></author><author><name sortKey="Fatemi, Mohammad Reza" sort="Fatemi, Mohammad Reza" uniqKey="Fatemi M" first="Mohammad Reza" last="Fatemi">Mohammad Reza Fatemi</name></author><author><name sortKey="Hong, Jun" sort="Hong, Jun" uniqKey="Hong J" first="Jun" last="Hong">Jun Hong</name></author><author><name sortKey="Poursasan, Najmeh" sort="Poursasan, Najmeh" uniqKey="Poursasan N" first="Najmeh" last="Poursasan">Najmeh Poursasan</name></author><author><name sortKey="Sheibani, Nader" sort="Sheibani, Nader" uniqKey="Sheibani N" first="Nader" last="Sheibani">Nader Sheibani</name></author><author><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></author></analytic><series><title level="j">International journal of biological macromolecules</title><idno type="eISSN">1879-0003</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Detergents (chemistry)</term><term>Dithiothreitol (chemistry)</term><term>Ecosystem</term><term>Fish Proteins (chemistry)</term><term>Fishes</term><term>Hemoglobins (chemistry)</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Oxidation-Reduction</term><term>Particle Size</term><term>Protein Binding</term><term>Protein Denaturation</term><term>Protein Stability</term><term>Quaternary Ammonium Compounds (chemistry)</term><term>Reducing Agents (chemistry)</term><term>Thermodynamics</term><term>Titrimetry</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Detergents</term><term>Dithiothreitol</term><term>Fish Proteins</term><term>Hemoglobins</term><term>Quaternary Ammonium Compounds</term><term>Reducing Agents</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Ecosystem</term><term>Fishes</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Oxidation-Reduction</term><term>Particle Size</term><term>Protein Binding</term><term>Protein Denaturation</term><term>Protein Stability</term><term>Thermodynamics</term><term>Titrimetry</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Varieties of hemoglobin (Hb) forms exist in fish, which are usually well adapted to the different ecological conditions or various habitats. In the current study, Hbs from two Sturgeon species of the Southern Caspian Sea Basin were purified and studied upon interaction with n-dodecyl trimethylammonium bromide (DTAB; as a cationic surfactant) by various methods including UV-visible absorption, dynamic light scattering (DLS), and ANS fluorescence spectrophotometry. The chemometric analysis of Hbs was investigated upon interaction with DTAB under titration, using UV-visible absorption spectra. The chemometric resolution techniques were used to determine the number of the components and mole fraction of the oxidized Hbs. These results provided the evidence for the existence of three different molecular components including native (N), intermediate (I) and denatured (D) in sturgeon Hbs. According to the distribution of intermediates, which were broadened in a range of DTAB concentration, the aggregation states, DLS experiments, and thermal stability (T(m) obtained by differential scanning calorimetry (DSC)), the Acipenser stellatus Hb was more stable compared to Acipenser persicus Hb. These results demonstrate a significant relationship between the stability of fish Hbs and the habitat depth requirements.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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