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 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

From animal hibernation to human’s hypometabolism: cellular mechanisms of natural and artificial hypobiosis

Objective: to carry out a comparative study of structural and functional responses of rats and hamsters RBCs when the animals entered and left an artificial hypobiosis state under conditions of hypothermia-hypoxia-hypercapnia.Мета: проведення порівняльних досліджень структурно-функціональної відповіді еритроцитів щурів та хом’яків на перебування тварин у стані штучного гіпобіозу за умов гіпотермії-гіпоксії-гіперкапнії та вихід з нього.Цель: провести сравнительные исследования структурно-функционального ответа эритроцитов крыс и хомяков на нахождение в состоянии искусственного гипобиоза в условиях гипотермии-гипоксии-гиперкапнии и выход из него