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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ariaeenejad, Shohreh Habibi-Rezaei, Mehran Kavousi, Kaveh Jamili, Shahla Fatemi, Mohammad Reza Hong, Jun Poursasan, Najmeh Sheibani, Nader Moosavi-Movahedi, Ali A. |
| Description | Country affiliation: Iran Author Affiliation: Ariaeenejad S ( Department of Marine Biology, Faculty of Marine Science and Technology, Science and Research Branch, Islamic Azad University, Tehran, Iran.) |
| 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. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| e-ISSN | 18790003 |
| DOI | 10.1016/j.ijbiomac.2012.10.015 |
| Journal | International Journal of Biological Macromolecules |
| Volume Number | 53 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-02-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Discipline Biochemistry Detergents Chemistry Fish Proteins Hemoglobins Protein Denaturation Quaternary Ammonium Compounds Animals Dithiothreitol Ecosystem Hydrophobic And Hydrophilic Interactions Oxidation-reduction Particle Size Protein Binding Protein Stability Reducing Agents Thermodynamics Titrimetry Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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