Физика Низких Температур: Том 43, Выпуск 6 (Июнь 2017), c. 898-901    ( к оглавлению , назад )

Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins

S.L. Rozanova, S.V. Narozhnyi, and O.A. Nardid

Department of Cryobiophysics, Institute for Problems of Cryobiology and Cryomedicine of the NAS of Ukraine 23 Pereyaslavska Str., Kharkiv 61015, Ukraine
E-mail: sv.rosanova@gmail.com; stas.narozhnyy@mail.ru

Received July 25, 2016


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.

PACS: 33.20.–t Molecular spectra;
PACS: 33.20.Lg Ultraviolet spectra;
PACS: 33.50.Dq Fluorescence and phosphorescence spectra.

Ключевые слова: albumin, hemoglobin, cytochrome C, freeze-thawing, antioxidant activity.

Published online: April 25, 2017