Inactivation of Gram (-) bacteria Salmonella enterica by chlorophyllin-based photosensitization: Mechanism of action and new strategies to enhance the inactivation efficiency.

This study is focused on the enhancement of susceptibility of Gram (-) bacteria S. enterica to chlorophyllin-based (Chl) photosensitization combining it with other antimicrobial tools. In order to find best combinations, the mechanism by which Chl-based photosensitization inactivates bacteria must be identified.

Molecular alterations in signal pathways of melanoma and new personalized treatment strategies: Targeting of Notch.

Despite modern achievements in therapy of malignant melanomas new treatment strategies are welcomed in clinics for survival of patients. Now it is supposed that personalized molecular therapies for each patient are needed concerning a specificity of molecular alterations in patient's tumors. In human melanoma, Notch signaling interacts with other pathways, including MAPK, PI3K-AKT, NF-kB, and p53.

Influence of osmotic shock on Escherichia coli insoluble protein fraction in the presence of exogenous osmolytes.

The influence of osmotic shock in the presence of exogenous osmolytes on the formation and composition of insoluble protein fraction in Escherichia coli was investigated. Interferon-α5 (IFN-α5) expressed in E. coli BL21(DE3) was used as a model protein.

Rat serum carboxylesterase partly hydrolyses gamma-butyrobetaine esters.

Although described some time ago, gamma-butyrobetaine esters and related compounds have not gained much attention from researchers, and their physiological function remains obscure. Formerly we detected GBB-esterase enzymatic activity in rat blood serum using phenylated gamma-butyrobetaine as an artificial substrate of the enzyme and HPLC. The aim of the present work was to develop an assay that would enable spectrophotometric or colorimetric determination of the reaction products of GBB-esterase activity and to reveal individual proteins performing GBB-esterase activity in rat blood serum.

Development-dependent changes in the tight DNA-protein complexes of barley on chromosome and gene level.

Background: The tightly bound to DNA proteins (TBPs) is a protein group that remains attached to DNA with covalent or non-covalent bonds after its deproteinisation. The functional role of this group is as yet not completely understood. The main goal of this study was to evaluate tissue specific changes in the TBP distribution in barley genes and chromosomes in different phases of shoot and seed development.

Mechanism of radiosensitization by porphyrins.

According to our previous data, hematoporphyrin dimethyl ether (HPde) at concentrations useful for photodynamic therapy can radiosensitize aggressive Ehrlich ascite carcinoma (EAT) to 2Gy irradiation inducing total tumour growth inhibition. The aim of this study was to further investigate the possible mechanism of radiosensitization of EAT by dicarboxylic porphyrin-HPde. Our results reveal that HPde is inducing several rearrangements in the EAT cells: 1.

Distribution of tight DNA-protein complexes along the barley chromosome 1H, as revealed by microsatellite marker analysis.

The distribution of DNA complexes with proteins resistant to routine deproteinisation procedures (tightly bound proteins, TBP) was studied on the barley chromosome 1H by means of microsatellite analysis. The polypeptide spectrum of the barley shoot TBP was similar to that formerly described for other organisms. In order to reveal developmental changes in the distribution of the TBP, DNA was extracted from dry grains, coleoptiles, root tips, and young and old leaves.