[Specialized software product for comparative analysis of multicomponent DNA fingerprints].

"GelAnalyzer" software, which is used to identify and correctly compare DNA fingerprints consisting of a large number of discrete bands, has been developed by the project to study the quantitative changes in DNA polymorphism patterns in animals and humans exposed to gamma radiation. The actual capabilities of this program are much broader and include the possibility to analyze the images of any multicomponent gels containing fragments of DNA, RNA, and proteins. This software product runs on Windows. "GelAnalyzer" allows one to analyze gel images obtained by a scanner, camera, or digital camera and ensures the visual control of the identification and comparative analysis of bands; it also makes it possible to take into account the bands that are poorly identified automatically and exclude the artifacts (incidental marks) on images. The operation of "GelAnalyzer" software is based on the determination of the values of normalized coordinates of bands with allowance for the relative electrophoretic mobility (Rf) of PCR products and comparison of their spectra (set of bands in gel lanes) to reveal the similarities or differences in their components with subsequent statistical data processing and display the results of the analysis.

[The dependence of stability of the green fluorescent protein-obelin hybrids on the nature of their constituent modules and the structure of the amino acid linker]. / Zavisimost' stabil'nosti gibridov zelenogo fluorestsentnogo belka s obelinom ot prirody sostavliaiushchikh ikh modulei i struktury aminokislotnogo linkera.

Recombinant plasmids containing genes for the green fluorescent protein (GFP) from Aequorea victoria and the photoprotein obelin from Obelia longissima linked in-frame by inserts differing in nucleotide sequences were constructed. The expression of the chimeric genes in Escherichia coli cells resulted in synthesis of the GFP-obelin hybrid proteins. These proteins were purified to homogeneity and subjected to limited trypsinolysis. It was shown that the resistance of GFP-obelin hybrid proteins to trypsin depends on the nature of their constituent modules and the amino acid sequences of linkers between the modules. The kinetics of accumulation of full-length hybrid proteins during the growth of bacterial cells does not depend on the structure of the peptide linkers. Most of the full-length product accumulates in cells in the form of inclusion bodies resistant to endogenous proteases. The soluble fraction of the protein undergoes considerable proteolysis regardless of the linker structure.