Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
enabled [disable] Abstract
Number of results

Results found: 2

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
EN
Proton exchange between spin groups of the solid matrix of hydrated granular potato starch and water was studied using the 2D time domain NMR. The proton spin-spin relaxation time T_2, and spin-lattice relaxation time T_1 (selective and non-selective pulse sequences) were measured at room temperature. The observed spin relaxation results were analysed for exchange assuming a two-site exchange model (between water and solid matrix of starch). In this analysis we determined the intrinsic spin-lattice relaxation time for water protons (49 ms) and solid starch matrix protons (172 ms), as well as the water-starch magnetization exchange rate (86 s^{-1}).
EN
Formation of free radicals in biological solutions leads to the changes in water protons relaxation times. Therefore, NMR relaxation measurements were used to investigate kinetics of oxidation processes induced by the addition, in low amounts, of hydrogen peroxide (H_2O_2) to aqueous protein solution and to blood serum. The measured relaxation times were not stable over time because of the progressive formation of free radicals and their damaging action to the protein structure. The addition of antioxidants (ascorbic acid, gallic acid etc.) changed the relaxation time courses due to free radical scavenging. Similar time courses, thus anti-oxidant actions, were observed in various blood serum without antioxidant additive. Moreover, the observed kinetics of spin-lattice relaxation time (T_1) depended on several factors, such as: structure and concentration of protein solutions and activity and concentration of the added antioxidants.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.