[Resistance of a hybridoma to the plant toxin viscumin does not depend on antibody affinity].
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Antibodies, Monoclonal↗
Biomedical subjects
N V Maliuchenko
Publications and source records attributed to N V Maliuchenko.
[Analysis of major antigenic determinants in Mistletoe lectin I].
Antigenic determinants of Mistletoe Lectin I, a toxin from Viscum album were predicted on the basis of the primary amino acid sequence of the protein. Based on the results of analysis, the peptide FPGGSTRTQARS, which corresponds to the 144-155 segment of the viscumin A-chain, was synthesized. The peptide was tested in enzyme-linked immunosorbent assay with monoclonal antibodies against the viscumin A-chain obtained previously. The peptide reacted with antibodies with a low affinity and did not inhibit the binding of viscumin molecule to any of the antibodies. Analysis of the peptide by 1H-NMR spectroscopy in aqueous solution was performed. The three-dimensional structure of the 144-155 segment in the native protein globule was shown.
Animals↗
[Unfolding of viscumin A-subunit during the intracellular transport of toxin].
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Animals↗
[Role of the interchain interaction domain of chain a in viscumin cytotoxicity].
The sequence coding for the viscumin (mistletoe lectin I, MLI) A-chain (MLA) was cloned from Viscum album genomic DNA with the use of synthetic primers. This yielded three recombinant (r) MLA variants differing in number of amino acid substitutions. The rMLA structure and properties were probed using monoclonal antibodies against native MLA. Native MLI B-chain (MLB) was shown to facilitate the rMLA folding. Native MLI and chimeric proteins consisting of rMLA and native MLB did not differ in cytotoxic effect on 3T3 fibroblastoid cells. Residues were identified that are located in the MLB-contacting region and have a considerable effect on the immunochemical and cytotoxic properties of rMLA.
3T3 Cells↗
[Structural features of proteins by intermittent-contact atomic force microscopy].
Optimal conditions of protein scanning by atomic force microscopy were developed. Proteins of different molecular masses (950-11.5 kDa) and different three-dimensional organization were used to investigate the structural features of proteins. The most distinct images of proteins were obtained using a tip with the free amplitude in the range of 5-15 nm and with the set-point amplitude in the regime of repulsion from the sample. The method allowed one to clearly recognize the structural details of large molecules such as immunoglobulins IgM and IgG1 and Ricinus agglutinin. The revealing of the structural properties of proteins with molecular masses of 60 kDa and less was limited by the sharpness of probe tips used in the present study. It was shown that, by a quantitative analysis of the geometric parameters of molecules, it is possible to distinguish IgG1, Ricinus agglutinin, and ricin.
Immunoglobulin G↗
[Detection of immune complexes using atomic force microscopy].
Complex formation between immunoglobulins and ligands immobilized on mica was studied by atomic force microscopy in two different systems. In the first system, 60-kDa ligands possessing only one site for antibody recognition were used. In the other system, a more complex interaction of human immunoglobulin with immobilized polyclonal antibodies was studied. In both systems, specific complexes with proper ligand appeared, and unspecific interaction was not detected. The method of revealing immunocomplexes by image atomic force microscopy can be used in the development of modern diagnostic systems.
Aluminum Silicates↗
[A quantitative analysis of complex formation between IgM and immobilized ligand using atomic force microscopy].
Specific interaction between human IgM and polyclonal antibodies immobilized on support was studied by atomic force microscopy. Human IgMs are responsible for a number of side effects arising during the xenotransplantation of mammalian organs to man. On the basis of atomic force microscopy, a quantitative analysis of complexes with IgM was performed. The data of the analysis agree well with the results of enzyme immunoassay. It was shown that the method of detection of immune complexes based on atomic force microscopy is able to detect specific antibodies/antigens in serum.
Aluminum Silicates↗
[Investigation of ribosomes of E. coli and T. maritima by atomic force microscopy].
Subunits 70S, 50S, and 30S of ribosomes of E. coli and T. maritima have been studied by atomic force microscopy. A considerable heterogeneity of structures was visualized when 70S and 30S subunits were sorbed on mica. The linear size and the height of molecules were estimated. It was found that the heights of ribosomes of E. coli and T. maritima substantially differ. The average height of 70S ribosomes of E. coli was 9.4 + 0.01 nm and that of T. maritima was 10.35 +/- 0.02 nm. The differences in the dimensions were probably determined by special organization of the mobile ribosomal element the L7/L12-stalk.
Escherichia coli↗