Исследование электрохимических свойств биологически-активных тиоловых соединений на золотоуглеродсодержащем электрод; Перспективы развития фундаментальных наук; Т. 2 : Химия
| Parent link: | Перспективы развития фундаментальных наук=Prospects of Fundamental Sciences Development: сборник научных трудов XV Международной конференции студентов, аспирантов и молодых ученых, г. Томск, 24-27 апреля 2018 г./ Национальный исследовательский Томский политехнический университет (ТПУ) ; под ред. И. А. Курзиной, Г. А. Вороновой.— , 2018 Т. 2 : Химия.— 2018.— [С. 72-74] |
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| Samenvatting: | Заглавие с экрана The electrochemical behavior of biologically active thiol compounds on a gold-carbon-containing electrode in solutions was investigated in order to suggest their model behavior with respect to ROS. It was found that the recovered forms of glutathione and cysteine exhibit different electrochemical properties depending on the method of removal of oxygen. In the presence of Na[2]SO[3], glutathione binds to the superoxide anion radical with the formation of disulfide and molecular oxygen. The disulfide form is reduced by Na[2]SO[3] to glutathione. This behavior is also characteristic of cysteine. In the presence of trace amounts of oxygen, if it is removed by bubbling with nitrogen, glutathione is oxidized by hydrogen peroxide to form a disulfide form. Disulfides of glutathione and cysteine are reduced on a gold-carbon-containing electrode at a potential of -1.0 V. |
| Taal: | Russisch |
| Gepubliceerd in: |
2018
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| Online toegang: | http://earchive.tpu.ru/handle/11683/50716 |
| Formaat: | Elektronisch Hoofdstuk |
| KOHA link: | https://koha.lib.tpu.ru/cgi-bin/koha/opac-detail.pl?biblionumber=627499 |
| Samenvatting: | Заглавие с экрана The electrochemical behavior of biologically active thiol compounds on a gold-carbon-containing electrode in solutions was investigated in order to suggest their model behavior with respect to ROS. It was found that the recovered forms of glutathione and cysteine exhibit different electrochemical properties depending on the method of removal of oxygen. In the presence of Na[2]SO[3], glutathione binds to the superoxide anion radical with the formation of disulfide and molecular oxygen. The disulfide form is reduced by Na[2]SO[3] to glutathione. This behavior is also characteristic of cysteine. In the presence of trace amounts of oxygen, if it is removed by bubbling with nitrogen, glutathione is oxidized by hydrogen peroxide to form a disulfide form. Disulfides of glutathione and cysteine are reduced on a gold-carbon-containing electrode at a potential of -1.0 V. |
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