Denaturation and intermediates study of two sturgeon hemoglobins by n-dodecyl trimethylammonium bromide.
Identifieur interne : 000274 ( PubMed/Curation ); précédent : 000273; suivant : 000275Denaturation 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></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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23142155</PMID><DateCreated><Year>2012</Year><Month>12</Month><Day>25</Day></DateCreated><DateCompleted><Year>2013</Year><Month>06</Month><Day>04</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>53</Volume><PubDate><Year>2013</Year><Month>Feb</Month></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int. J. Biol. Macromol.</ISOAbbreviation></Journal><ArticleTitle>Denaturation and intermediates study of two sturgeon hemoglobins by n-dodecyl trimethylammonium bromide.</ArticleTitle><Pagination><MedlinePgn>107-13</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2012.10.015</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(12)00412-6</ELocationID><Abstract><AbstractText>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.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier B.V. All rights reserved.</CopyrightInformation></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, Tehran, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Habibi-Rezaei</LastName><ForeName>Mehran</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kavousi</LastName><ForeName>Kaveh</ForeName><Initials>K</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>Hong</LastName><ForeName>Jun</ForeName><Initials>J</Initials></Author><Author 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