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891.
Co-administration of Selenium with Inorganic Mercury Alters the Disposition of Mercuric Ions in Rats
Orr Sarah E. George Hannah S. Barnes Mary C. Mathis Taylor N. Joshee Lucy Barkin Jennifer Kiefer Adam M. Seney Caryn S. Bridges Christy C. 《Biological trace element research》2020,195(1):187-195
Biological Trace Element Research - Mercury (Hg) is a common environmental toxicant to which humans are exposed regularly through occupational and dietary means. Although selenium supplementation... 相似文献
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Calabrò Marco Mandelli Laura Crisafulli Concetta Porcelli Stefano Albani Diego Politis Antonis Papadimitriou George N. Di Nicola Marco Janiri Luigi Colombo Roberto Martinotti Giovanni Bellomo Antonello Vieta Eduard Bonassi Stefano Frustaci Alessandra Ducci Giuseppe Landi Stefano Boccia Stefania Serretti Alessandro 《Molecular biology reports》2020,47(1):191-200
Molecular Biology Reports - Serotoninergic system is one of the most important neurotransmission systems investigated in the field of psychiatry. Extensive evidence reveals how alterations of this... 相似文献
894.
Ludmila Aricov Daniel George Angelescu Adriana Băran Vlad Tudor Popa Aurica Precupaş 《Journal of biomolecular structure & dynamics》2020,38(9):2659-2671
AbstractThe binding of drugs to serum proteins is governed by weak non-covalent forces. In this study, the nature and magnitude of the interactions between piroxicam (PRX) and bovine serum albumin (BSA) was assessed using spectroscopic, calorimetric and computational molecular methods. The fluorescence data revealed an atypical behavior during PRX and BSA interaction. The quenching process of tryptophan (Trp) by PRX is a dual one (approximately equal static and dynamic quenched components). The FRET results indicate that a non-radiative transfer of energy occurred. The association constant and the number of binding sites indicate moderate PRX and BSA binding. The competitive binding study indicates that PRX is bound to site I from the hydrophobic pocket of subdomain IIA of BSA. The synchronous spectra showed that the microenvironment around the BSA fluorophores and protein conformation do not change considerably. The Trp lifetimes revealed that PRX mainly quenches the fluorescence of Trp-213 situated in the hydrophobic domain. The CD and DSC investigation show that addition of PRX stabilizes the protein structure. ITC results revealed that BSA-PRX binding involves a combination of electrostatic, hydrophobic and hydrogen interactions. The analysis of the computational data is consistent with the experimental results. This thorough investigation of the PRX-BSA binding may provide support for other studies concerning moderate affinity drugs with serum protein.Communicated by Ramaswamy H. Sarma 相似文献
895.
Hydrostatic pressure has a vital role in the biological adaptation of the piezophiles, organisms that live under high hydrostatic pressure. However, the mechanisms by which piezophiles are able to adapt their proteins to high hydrostatic pressure is not well understood. One proposed hypothesis is that the volume changes of unfolding (ΔVTot) for proteins from piezophiles is distinct from those of nonpiezophilic organisms. Since ΔVTot defines pressure dependence of stability, we performed a comprehensive computational analysis of this property for proteins from piezophilic and nonpiezophilic organisms. In addition, we experimentally measured the ΔVTot of acylphosphatases and thioredoxins belonging to piezophilic and nonpiezophilic organisms. Based on this analysis we concluded that there is no difference in ΔVTot for proteins from piezophilic and nonpiezophilic organisms. Finally, we put forward the hypothesis that increased concentrations of osmolytes can provide a systemic increase in pressure stability of proteins from piezophilic organisms and provide experimental thermodynamic evidence in support of this hypothesis. 相似文献
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