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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Antonov, Y. A. Zhuravleva, I. L. |
| Description | Country affiliation: RUSSIA Author Affiliation: Antonov YA ( N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Kosygin Stir. 4. 119334 Moscow, Russia. chehonter@yandex.ru) |
| Abstract | We study the effect of limited heat-induced aggregation of BSA on structure development in the water-gelatin-thermally aggregated BSA (BSA(TA)) system. The pH is set at 5.4 and the temperature is higher than the conformation transition temperature of gelatin, but lower than the denaturation temperature of BSA. Dynamic light scattering, circular dichroism, and fluorescence measurements are used to monitor structure changes. Interaction of gelatin with BSA(TA) leads to formation of large complex particles with an average radius â¼1500 nm. BSA-gelatin complex formation accompanies partial destabilization of the secondary and tertiary structures of BSA and an additional exposure of hydrophobic tryptophan residues on the surface of the globule. It is shown that electrostatic interaction of the oppositely charged groups of BSA(TA) and gelatin is responsible for formation of such complex particles, whereas the secondary forces (hydrophobic interaction and hydrogen bonds) play an important role in stabilization of the complex particles. The zeta potentials of the native and the thermally aggregated BSA samples were determined, and the solvent quality has been quantified by determining the activity of the protein samples in their saturated solutions. It was shown that steric reasons (large size of the thermally aggregated BSA(TA) particles), and uncomplete charge compensation of the positively charged gelatin molecules by the negatively charged BSA(TA) particles are the main factors in determining structure formation, while the levels of the activity of the native BSA and BSA(TA) have a smaller effect on the structure of complex. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 53 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-02-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Gelatin Chemistry Serum Albumin, Bovine Animals Cattle Circular Dichroism Light Particle Size Polyethylene Glycols Protein Binding Protein Multimerization Protein Stability Protein Structure, Secondary Scattering, Radiation Sodium Chloride Solubility Spectrometry, Fluorescence Journal Article |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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