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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| Veröffentlicht in: | Физика низких температур |
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| Datum: | 2017 |
| ISSN: | 0132-6414 |
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | Englisch |
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Фізико-технічний інститут низьких температур ім. Б.І. Вєркіна НАН України
2017
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| Online Zugang: | 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 |
| Zitieren: | 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. |
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Digital Library of Periodicals of National Academy of Sciences of Ukraine| Zusammenfassung: | 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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| ISSN: | 0132-6414 |