Laser correlation spectroscopy of the processes of serum albumin denaturation
| Autor: | V. E. Mikrin, A. M. Saletskii, A. N. Baranov, I. M. Vlasova |
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| Rok vydání: | 2004 |
| Předmět: |
Chromatography
biology Albumin Serum albumin Analytical chemistry Buffer solution Condensed Matter Physics Micelle chemistry.chemical_compound Isoelectric point Pulmonary surfactant chemistry biology.protein Denaturation (biochemistry) Two-dimensional nuclear magnetic resonance spectroscopy Spectroscopy |
| Zdroj: | Journal of Applied Spectroscopy. 71:911-915 |
| ISSN: | 1573-8647 0021-9037 |
| DOI: | 10.1007/s10812-005-0021-9 |
| Popis: | Denaturation of serum albumin under the influence of temperature and ionic detergent sodium dodecylsulfate (SDS) is investigated by laser correlation spectroscopy of scattered light. It is shown that thermal denaturation is stronger at pH values of the buffer solution of protein that are close to the isoelectric point of the given protein. Coupling of the micelles of SDS with albumin follows the principle of positive cooperativity. The concentration of protein saturation with the surfactant is determined, upon the attainment of which further protein denaturation was not observed. It is shown that the interaction of SDS with albumin is of an electrostatic nature. |
| Databáze: | OpenAIRE |
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