Serum albumin molecular mobility in water solutions, containing iron chloride III
Paper #3128 received 2016.11.20; accepted for publication 2016.12.29; published online 2016.12.31.
1. P. T. Lieu, M. Heiskala, P. A. Peterson, and Y. Yang, “The roles of iron in health and disease,” Molecular Aspects of Medicine 22(1–2), 1–87 (2001).
2. Z. Shu-hong, F. Yong-shan, F. Shuo, and Z. Yun-feng, “Microdetermination of proteins by resonance light scattering technique based on aggregation of ferric nanoparticles,” Spectrochimica Acta Part A 72, 748–752 (2008). Crossref
3. B. D. Fair, and A. M. Jamieson, “Effect of Electrodynamic Interactions on the Translational Diffusion of Bovine Serum Albumin at Finite Concentration,” Journal of Colloid and Interface Science 73(1), 130-135 (1980). Crossref
4. M. Othman, A. Aschi, and A. Gharbi, “Polyacrylic acids–bovine serum albumin complexation: Structure and dynamics,” Materials Science and Engineering C. 58, 316-323 (2016). Crossref
5. V. V. Gibizova, I. A. Sergeeva, G. P. Petrova, A. V. Priezzhev, and N. G. Khlebtsov, “Interaction of Albumin and gamma-Globulin Molecules with Gold Nanoparticles in Water Solutions,” Moscow University physics bulletin. 66(5), 449–452 (2011) [in Russian].
7. H. Z. Cummins, and E. R. Pike, Photon Correlation and Light Beating Spectroscopy, Springer Science+Business Media, New York (1974). Crossref
8. A. Einstein, Collected Papers, Nauka, Moscow (1966) [in Russian].
9. V. N. Tsvetkov, B. E. Eskin, and S. Y. Frenkel, Structure of Macromolecules in Solutions, Nauka, Moscow (1964) [in Russian].
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