Suchergebnisse

For human and chicken lysozyme , the relationship between changes in the parameters of enzyme adsorption on living Escherichia coli bacterial cells and the value of its effective bacteriolytic activity in the presence of glycine and charged amino acids was studied . It has been shown for both human and chicken lysozyme that free amino acids added to a concentration of 1.5 mM for glycine or 5.0 mM for glutamate, aspartate, histidine, arginine, and lysine reduce the desorption constant of the enzyme on bacterial cells to 1.4-2.0 times. At the same time, an increase in the bacteriolytic activity of lysozyme is also observed in 1.5-1.9 times. Thus, the enhancement of antibacterial activity in the presence of glycine and charged amino acids can be explained by an improvement in the productive sorption of the enzyme on the substrate, bacterial cells.

E. coli strains have been created as producers of recombinant β1-adreno-receptor epitopes as part of chimeric proteins. The corresponding epitope sequences are located in the C-terminal region of the human heart fatty acid binding protein (hH-FABP) and separated from it by a linker sequence (Gly4Ser)3. A solid-phase enzyme-linked immunosorbent assay (ELISA) for detection of autoantibodies against β1-adrenergic receptor in human blood serum based on a recombinant epitope has been developed. Blood sera of patients (N = 76) with various diagnoses of cardiopathologies and other diseases were analyzed. In some patients with a con rmed diagnosis of cardiovascular diseases, a signi cantly increased level of autoantibodies to β1-adrenergic receptor was detected, in most cases those with a diagnosis of acute myocardial infarction.