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82 results for “Thiol”

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zenodo16/100

Effects of thiol substitution in low-transition-temperature mixtures (LTTMs) as solvents for metal oxides

<p>This study deals with an investigation of how substitution of an alcohol group by a thiol group in mixtures of choline chloride with a series of bio-sourceable molecules affects the physico-chemical properties of the mixtures and their ability to dissolve metal oxides. All of the thiol mixtures studied showed a higher affinity and selectivity for late transition metals and the physical properties of the mixtures were improved compared to their alcohol analogues (<em>i.e.</em> lower viscosity, wider liquid range). The metal solubility was assessed<em> via </em>determinination of the final concentration of the metal oxides dissolved in thiol mixtures<em> via </em>inductively coupled plasma optical emission spectroscopy (ICP-OES). The thiol function selectively improved the solubilities of the late transition metal oxides (<em>i.e.</em> copper and zinc), which are valuable metals often present as residue in industrial waste. The solubility of iron oxides was much lower than that of the valuable metals, which is a significant benefit in industrial applications. The different solubilization behaviour of metal oxides in the thiol and alcohol mixtures was further investigated<em> via </em>UV-vis absorption and infrared spectroscopy. This study allowed to assess the potential of these low-temperature-transition mixtures for the selective recovery of metals.</p>

restrictedApr 2020View details →
zenodo12/100

Data related to the article "N-Acetyl-Cysteine Regenerates Albumin Cys34 by a Thiol-Disulfide Breaking Mechanism: An Explanation of Its Extracellular Antioxidant Activity"

<p>This record contains raw data related to the article &ldquo;N-Acetyl-Cysteine Regenerates Albumin Cys34 by a Thiol-Disulfide Breaking Mechanism: An Explanation of Its Extracellular Antioxidant Activity&rdquo;</p> <p><strong>Abstract</strong></p> <p>In the present paper, the extracellular antioxidant activity of N-acetyl-cysteine (NAC) is explained by considering its ability to regenerate the free form of albumin Cys34 by breaking the disulfide bond of the cysteinylated form (HSA-Cys). NAC&rsquo;s capability to regenerate albumin Cys34 (HSA-SH) was studied by MS intact protein analysis in human plasma and in a concentration range of NAC easily achievable after oral and i.v. administration (5&ndash;50 &micro;g/mL). NAC dose-dependently broke the HSA-Cys bond to form the dimer NAC-Cys thus regenerating Cys34, whose reduced state was maintained for at least 120 min. Cys was faster in restoring Cys34, according to the reaction constant<br> determined with the glutathione disulfide (GSSG) reaction, but after 60 min the mixed disulfide HSA-Cys turned back due to the reaction of the dimer Cys-Cys with Cys34. The explanation for the different rate exchanges between Cys-Cys and Cys-NAC with Cys34 was given by molecular modelling studies. Finally, the Cys34 regenerating effect of NAC was related to its ability to improve the total antioxidant capacity of plasma (TRAP assay). The results well indicate that NAC greatly increases the plasma antioxidant activity and this effect is not reached by a direct effect but through the regenerating effect of Cys34.</p>

restrictedDec 2020View details →

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Last verified 2026-04-29Open record