[THE USE OF THE COMMERCIAL APPARATUS DUAL GEL MODULE FOR THE TWO-DIMENSIONAL POLYACRYLAMIDE GEL ELECTROPHORESIS].

Two-dimensional gel electrophoresis, continues to be one of the fundamental methods to study the biological protein diversity. This method described by O'Farrell in 1975 includes two following steps: isoelectric focusing in the first dimension and polyacrylamide gel electrophoretic fractionation of proteins according to their molecular weight in the second dimension. In this manuscript we described several technical parameters of the commercial apparatus Dual Gel Module for the gel electrophoresis by means of which it is possible to accomplish the electrophoretic protein fractionation in both dimensions.

[Mass-spectrometric analysis of proteasomal subunits possessing endoribonuclease activity].

Proteasomes act as the main apparatus of non-lysosomal intracellular proteolysis and participate in the regulation of most important cellular processes. Despite considerable progress in the understanding of proteasome's functioning, some issues, in particular, RNase activity of these ribonucleoprotein complexes and its regulation remain scarcely explored. In this paper we found several proteins corresponding by electrophoretic mobility to subunits of the complex 20S proteasome to possess endoribonuclease activity with respect to both sense and antisense sequences of the c-myc mRNA 3'-UTR.

[The potential of three-dimensional simulation as the method for situational reconstruction of the gunshot injury mechanism].

A method for the three-dimensional modeling is proposed designed to enhance the objective value of situational expert investigations of the mechanism of gunshot wounds. The method was successfully validated in a number of forensic medical situational studies and allowed their objectiveness, demonstrativeness, and evidentiary force to be significantly improved.

[Proteasomes and their role in the extracellular space].

The presented review concerns the intracellular proteasome and their possible functions. The ubiquitin-proteasome system (UPS) is responsible for the common regulated proteolysis in the cell. 26S proteasome is a central proteolytic unit of UPS and is a multisubunit protein complex consisting of a core catalytic complex, called 20S proteasome, capped at one or both ends by 19S regulatory complex.

[Comparative analysis of methods for purification and concentration of 26S proteasomes isolated from rat liver].

The 26S proteasome is a multi-subunit protein complex that consists of the catalytic 20S and regulatory 19S sub-complexes. The most well studied function of proteasomes is specific degradation of proteins. There are several purification schemes for obtaining the preparations of 26S proteasomes.