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Isaeva A. I. Maikov E. Gibizova V. V. Petrova G. P. 《Journal of Applied Spectroscopy》2021,88(4):789-793
Journal of Applied Spectroscopy - Aqueous solutions of human hemoglobin have been studied by the multi-angle static light scattering method. The tendency of sickle-shaped erythrocytes to aggregate... 相似文献
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V. V. Gibizova I. A. Sergeeva G. P. Petrova A. V. Priezzhev N. G. Khlebtsov 《Moscow University Physics Bulletin》2011,66(5):449-452
The molecular mobility of scattering particles in water solutions of albumin and γ-globulin proteins with gold nanoparticles
was investigated by the dynamic light scattering method. The dependences of translation diffusion coefficients of particles
at various concentrations of the solution components have been obtained. It was revealed that in a wide range of concentrations
of the solution components there is no interaction of gold nanoparticles with albumin, whereas gold nanoparticles form complexes
with γ-globulin molecules. 相似文献
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I. A. Sergeeva E. A. Shirshin N. G. Zhdanova V. V. Gibizova G. P. Petrova S. A. Kurguzenkov V. V. Fadeev 《Optics and Spectroscopy》2013,115(2):171-176
The effect of lead (heavy metal) cations on the fluorescence characteristics and photophysical parameters (fluorescence intensity and anisotropy, absorption cross section, excited state lifetime, and rates of singlet-triplet conversion and reversible photobleaching) of tryptophan in an aqueous solution of bovine serum albumin (two-tryptophan protein) is studied and compared with the effect in the aqueous solution of tryptophan. It is demonstrated that the effect of lead on the fluorescence characteristics of the protein is manifested at a molar concentration ratio of metal cations and protein macromolecules of greater than 10 and related to the dynamic quenching of the excited state, protein aggregation, and an increase in the rate of singlet-triplet conversion (the effect of a heavy atom) in tryptophan molecules. 相似文献
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K.?A.?AnenkovaEmail author G.?P.?Petrova V.?V.?Gibizova L.?A.?Osminkina K.?P.?Tamarov 《Optics and Spectroscopy》2013,115(2):166-170
The interaction of molecules of bovine serum albumin (BSA) with silicon nanoparticles (SiNPs) was studied in water solutions of them at different pH values. The data of photon correlation spectroscopy and IR spectroscopy of studied solutions indicate the absence of interaction between BSA and SiNPs in the pH range 3–7, which is attested to by the experimentally obtained character of the pH dependence of the translational diffusion coefficient D t and by the absence of hydrogen bonds between the protein carbonyl groups and the OH groups on the surface of mesoporous silicon nanoparticles. The obtained data may play a leading role in further in vivo application of silicon nanoparticles. 相似文献
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