«Актуальные вопросы в сфере социально-экономических, технических и естественных наук и информационных технологий» (3-4 апреля 2014г.)

Zhyltsova A. S., Saevich O. V., Posudiievska O. R.

Oles Honchar Dnipropetrovsk National University


Serum albumin is one of the major plasma proteins. It is a convenient object of study, as levels of its structural organization were transcribed and it’s important functions, performed in the human body, are also known. The equilibrium state of a protein molecule provides the presence of active binding sites in albumin. That’s why albumin possesses a unique ability to bind a large number of different substances. It should be noted that the impact of physical field of any nature can lead to modification of albumin molecules. Along with that, the parameters of the field will be of the main importance. By varying the parameters of the field, it is possible to obtain a certain degree of modification of albumin molecules and, accordingly to control one of its main functions – transportation of physiological metabolites.

The aim of the research was to investigate the influence of physical fields of different nature on a model system «albumin – water», as well as the definition of modification of biopolymer molecules, depending on the intensity of field action.

The object of our study was the model systems of human serum albumin in the concentration range of 0.5–1 %. Microwave exposure was determined in a microwave oven Elenberg MS-2010D (900 Watts). It has been stated that the increase in exposure time of albumin solution from 1 to 3 minutes leads to the increase in the degree of modification of its molecules from 15 % to 97 % respectively. Along with the increasing concentration of albumin in the model system the degree of modification of its molecules ranges from 7 % to 65 % at 1 and 3 minutes of microwave exposure. It is shown that the microwave field has a considerable effect on the modification of biopolymer molecules and, together with the increase in exposure time, it can lead to the biopolymer’s almost complete denaturation.