Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins
The purpose of the present work was to investigate influence of different freeze-thawing protocols on structure and antioxidant properties of isolated proteins. In our experiments we have studied human serum albumin, human hemoglobin and cytochrome C derived from equine heart frozen down to 77.15 K...
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| Опубліковано в: : | Физика низких температур |
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| Дата: | 2017 |
| Автори: | , , |
| Формат: | Стаття |
| Мова: | Англійська |
| Опубліковано: |
Фізико-технічний інститут низьких температур ім. Б.І. Вєркіна НАН України
2017
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| Онлайн доступ: | https://nasplib.isofts.kiev.ua/handle/123456789/129506 |
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| Назва журналу: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| Цитувати: | Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins / S.L. Rozanova, S.V. Narozhnyi, O.A. Nardid // Физика низких температур. — 2017. — Т. 43, № 6. — С. 898-901. — Бібліогр.: 18 назв. — англ. |
Репозитарії
Digital Library of Periodicals of National Academy of Sciences of Ukraine| _version_ | 1862716100128538624 |
|---|---|
| author | Rozanova, S.L. Narozhnyi, S.V. Nardid, O.A. |
| author_facet | Rozanova, S.L. Narozhnyi, S.V. Nardid, O.A. |
| citation_txt | Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins / S.L. Rozanova, S.V. Narozhnyi, O.A. Nardid // Физика низких температур. — 2017. — Т. 43, № 6. — С. 898-901. — Бібліогр.: 18 назв. — англ. |
| collection | DSpace DC |
| container_title | Физика низких температур |
| description | The purpose of the present work was to investigate influence of different freeze-thawing protocols on structure and antioxidant properties of isolated proteins. In our experiments we have studied human serum albumin, human hemoglobin and cytochrome C derived from equine heart frozen down to 77.15 K with 1–2 deg/min and 300 deg/min rate with following thawing on a water bath at 293.15 K. Native proteins were assumed as a control. Influence of freeze-thawing protocols on protein structure was investigated using spectrophotometric and fluorescent assays. Antioxidant activities of isolated proteins were estimated by their ability to reduce ABTS ⁺ radical. It has been established that unfolding derived from freeze-thawing exposure leads to protein antioxidant activity increasing while decreasing of such an activity may be connected with macromolecule aggregation. Character of freeze-thawing influence on antioxidant activity of proteins depends on molecule structure peculiarities and freezing protocols.
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| first_indexed | 2025-12-07T18:03:04Z |
| format | Article |
| fulltext | |
| id | nasplib_isofts_kiev_ua-123456789-129506 |
| institution | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| issn | 0132-6414 |
| language | English |
| last_indexed | 2025-12-07T18:03:04Z |
| publishDate | 2017 |
| publisher | Фізико-технічний інститут низьких температур ім. Б.І. Вєркіна НАН України |
| record_format | dspace |
| spelling | Rozanova, S.L. Narozhnyi, S.V. Nardid, O.A. 2018-01-19T20:23:51Z 2018-01-19T20:23:51Z 2017 Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins / S.L. Rozanova, S.V. Narozhnyi, O.A. Nardid // Физика низких температур. — 2017. — Т. 43, № 6. — С. 898-901. — Бібліогр.: 18 назв. — англ. 0132-6414 PACS: 33.20.–t, 33.20.Lg, 33.50.Dq https://nasplib.isofts.kiev.ua/handle/123456789/129506 The purpose of the present work was to investigate influence of different freeze-thawing protocols on structure and antioxidant properties of isolated proteins. In our experiments we have studied human serum albumin, human hemoglobin and cytochrome C derived from equine heart frozen down to 77.15 K with 1–2 deg/min and 300 deg/min rate with following thawing on a water bath at 293.15 K. Native proteins were assumed as a control. Influence of freeze-thawing protocols on protein structure was investigated using spectrophotometric and fluorescent assays. Antioxidant activities of isolated proteins were estimated by their ability to reduce ABTS ⁺ radical. It has been established that unfolding derived from freeze-thawing exposure leads to protein antioxidant activity increasing while decreasing of such an activity may be connected with macromolecule aggregation. Character of freeze-thawing influence on antioxidant activity of proteins depends on molecule structure peculiarities and freezing protocols. en Фізико-технічний інститут низьких температур ім. Б.І. Вєркіна НАН України Физика низких температур Низкоразмерные и неупорядоченные системы Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins Article published earlier |
| spellingShingle | Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins Rozanova, S.L. Narozhnyi, S.V. Nardid, O.A. Низкоразмерные и неупорядоченные системы |
| title | Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins |
| title_full | Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins |
| title_fullStr | Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins |
| title_full_unstemmed | Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins |
| title_short | Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins |
| title_sort | influence of freezing down to 77.15 k on structure and antioxidant power of some proteins |
| topic | Низкоразмерные и неупорядоченные системы |
| topic_facet | Низкоразмерные и неупорядоченные системы |
| url | https://nasplib.isofts.kiev.ua/handle/123456789/129506 |
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