Determination of the parameters of the rotational diffusion of complexes of serum albumins with Triton X-100 from analysis of tryptophan fluorescence
| Autor: | I. M. Vlasova, V. V. Zhuravleva, Alexander M. Saletsky |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Chromatography
biology Chemistry Diffusion Analytical chemistry Rotational diffusion Human serum albumin chemistry.chemical_compound Isoelectric point Pulmonary surfactant Critical micelle concentration Triton X-100 biology.protein medicine Physical and Theoretical Chemistry Bovine serum albumin medicine.drug |
| Zdroj: | Russian Journal of Physical Chemistry B. 7:562-567 |
| ISSN: | 1990-7923 1990-7931 |
| DOI: | 10.1134/s1990793113050369 |
| Popis: | The rotational diffusion of complexes of human serum albumin (HSA) and bovine serum albumin (BSA) with neutral surfactant Triton X-100 is study by analyzing the polarized tryptophan fluorescence and its parameters are determined (rotational relaxation time, diffusion coefficient, effective radius). Similarities in the solubilization of both proteins are revealed: an effective solubilization BSA and HSA in solutions containing neutral surfactant Triton X-100 is achieved at concentration of the latter of 0.3 mM, slightly greater than its critical micelle concentration (0.25 mM), with the most significant effect taking place at pH 5.0, a value close to the isoelectric points of the proteins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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