Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins
DOI (Low Temperature Physics):
https://doi.org/10.1063/1.4985979Ключові слова:
albumin, hemoglobin, cytochrome C, freeze-thawing, antioxidant activity.Анотація
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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Опубліковано
2017-04-13
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S.L. Rozanova, S.V. Narozhnyi, and O.A. Nardid, Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins, Low Temp. Phys. 43, (2017) [Fiz. Nizk. Temp. 43, 898-901, (2017)] DOI: https://doi.org/10.1063/1.4985979.
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Низькоpозмірні та невпорядковані системи
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