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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.

A technique for lateral ow hybridization analysis of speci c bacterial beta-lactamase mRNAs has been developed, including the preparation of a biotinylated target DNA and its analysis on a test strip with immobilized oligonucleotide probes. When the DNA target and probe structures are complementary, DNA duplexes are formed in the test zone of the strip, which interact with the streptavidin conjugate with gold nanoparticles. The method was used to determine the transcripts of the TEM-type betalactamase genes isolated from the culture of E. coli - producers of the corresponding recombinant betalactamase. It has been shown that singlestranded DNA target of 330 bases was revealed most effectively in lateral ow analysis.