[Psychological assessment of visual hemispatial neglect: standardization and approbation of the modified digit cancellation test].

Aim: To study the phenomena of visual-hemispatial neglect in healthy people and patients with brain diseases of different genesis.

Material And Methods: Eighty-eight patients with schizophrenia spectrum disorders, 68 patients with exogenous organic brain diseases and 240 healthy adults of different age were included in the study. The digit cancellation test modified by the authors was used.

Characterization of antigenic properties of horseradish peroxidase with monoclonal antibodies.

Monoclonal antibodies (mcAbs) specific to alkaline isoenzymes of horseradish peroxidase were used to characterize the antigenic properties of horseradish peroxidase. The results of a competitive binding assay indicated that monoclonal antibodies can be divided into three groups directed against distinct parts of the protein. The interaction of monoclonal antibodies with native and modified horseradish peroxidase showed also three different patterns of reactivity.

[Effect of degree of aerosol OT reverse micelle hydration on the catalytic activity of peroxidase, its conjugate with cortisol and their immune complexes].

In Aerosol OT (AOT) reversed micelles in heptane, the oxidation kinetics of ortho-phenylenediamine (PDA) catalyzed by peroxidase (HRP), its conjugate with nine cortisol molecules and their immunocomplexes with monoclonal antibodies AT-2C specific to domain I of HRP has been studied with regard to the hydration degree of micelles W(0) = [H2O]/[A0T] and the concentration of solubilized biocatalysts. The profiles of dependencies of the initial PDA oxidation rate, v(0), on W(0) varied with an increase in the concentrations of HRP, HRP-cortisol and their immunocomplexes in micellar systems. The rise in HRP concentration from 0.

[Solid-phase methods of immunoenzyme analysis of the herbicides simazine and atrazine].

Competitive methods of enzyme immuno assay (EIA) for detecting simazine and atrazine were developed, and conditions providing optimal performance were found. EIA sensitivity was shown to increase by an order of magnitude if samples were preincubated with antibodies; chloride ions were omitted; a herbicide-peroxidase conjugate was treated with urea. In EIA using labelled antibodies sensitivities thresholds towards simazine and atrazine were 0.

[The effect of monoclonal and polyclonal antibodies to peroxidase on combined peroxidase oxidation of 4-iodophenol with luminol and 4-aminoantipyrine].

The kinetics of peroxidase-dependent cooxidation for two substrate pairs [p-iodophenol + 4-aminoantipyrine (AAP) and p-iodophenol + luminol was studied both in the absence and presence of polyclonal antibodies (polyAB), three types of peroxidase-specific monoclonal antibodies (monoAB) and their double or triple mixtures in a wide range of H2O2 concentrations (0.01-10.0 mM).

[Interaction of monoclonal antibodies with horseradish peroxidase].

Properties of four types of monoclonal antibodies to horse-radish peroxidase were investigated. The dissociation constants and molecular-weight composition of the immune complexes were determined. The antibodies are shown to be directed to different epitopes on the polypeptide chain.

[Changes in the adiabatic compressibility of mono- and polyclonal antibodies during interaction with antigens].

The values of apparent adiabatic compressibility of free and antigen-bound antibodies were determined by means of precise density and ultrasound velocity measurements. It was shown that during the formation of soluble immune complexes (insulin--monoclonal antibodies to insulin and alpha-amylase--monovalent Fab-fragments of antibodies to alpha-amylase), the apparent compressibility of antibodies decreased by (0.3 divided by 0.

Mapping of the immunodominant regions of the NAD-dependent formate dehydrogenase.

A panel of 4 monoclonal antibodies and 7 polyclonal antisera against NAD-dependent formate dehydrogenase from methylotrophic bacterium Pseudomonas sp. 101 has been obtained. The reactivity of the 37 overlapping proteolytic peptides with the monoclonal antibodies and polyclonal antisera has been studied with ELISA test.

[Isolation and characterization of monoclonal antibodies to horseradish peroxidase].

Monoclonal antibodies to horseradish peroxidase were obtained. The interaction of two antibody clones with the enzyme was studied. Antibodies of one clone were found to inhibit the enzyme activity during the oxidation of 2.

[Cooperative effects during interaction of monoclonal antibodies with insulin dimers].

The interaction of monoclonal antibodies of three types with the ATP-labeled insulin dimer was studied by the luminescent immunocofactor method. It was shown that the effective equilibrium binding constant increases at equimolar antigen/antibody concentrations. This can be due to the formation of multimolecular complexes between the antigens and antibodies.

[Preparation of an insulin conjugate with beta-galactosidase from E. coli for immunoenzyme assay].

A modified procedure has been worked out for preparing a conjugate of porcine insulin with E. coli beta-galactosidase employing a heterobifunctional reagent, N-hydroxysuccinimidyl m-maleimidobenzoate. Optimal conditions for insulin acylation and subsequent coupling with beta-galactosidase were selected that afforded the conjugate in a high yield.

Study of the monoclonal antibody-insulin interaction.

We generated four stable hybridoma lines producing monoclonal antibodies. All antibodies were as reactive with insulin from other species as with swine insulin. The apparent affinity of the monoclonal antibodies for insulin varied in the range from 2 X 10(8) M-1 to 2 X 10(10) M-1.

[Effect of specific antibodies on association of glyceraldehyde 3-phosphate dehydrogenase subunits].

The rabbit antibodies against glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.

[Use of immobilization for investigation of glyceraldehyde 3-phosphate dehydrogenase. Immobilized tetramers].

Glyceraldehyde-3-phosphate dehydrogenase from yeast and rat skeletal muscle was covalently linked to CNBr-activated Sepharose 4B. When the activation was as high as 4-5 mg of CNBr per ml of Sepharose, the enzymes had their maximal activity and were linked to the carrier only by one of the four subunits. The specific activity of immobilized dehydrogenases makes up to 50-60% of that of soluble preparations, since the rate of the substrate diffusion into Sepharose granules is too low.

Study of subunit interactions in immobilized D-glyceraldehyde-3-phosphate dehydrogenase.

Under conditions which cause dissociation of soluble tetrameric glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.2.1.

[Immobilization of glyceraldehyde-3-phosphate dehydrogenase by non-covalent binding to specific antibodies and Fab-fragments coupled to Sepharose].

Rabbit antibodies to rat skeletal muscle glyceraldehyde-3-phosphate dehydrogenase, as well as monovalent Fab fragments of these antibodies were coupled to CNBr-activated Sepharose 4B. Rat skeletal muscle glyceraldehyde-3-phosphate dehydrogenase was then immobilized on a matrix by non-covalent binding to specific antibodies. Immobilized enzyme retains approximately 90% catalytic activity of the soluble dehydrogenase; pH optimum of activity and the Km value observed are changed as compared to the enzyme in solution.

[Enzymatic splitting of antibodies bound to immobilized antigen as a means of Fab fragments preparation].

A method of Fab fragments preparation by enzymatic splitting of antibodies bound to specific antigen immobilized on an insoluble support is described. The complex of rat muscle glyceraldehyde-3-phosphate dehydrogenase (GAPD), immobilized on Sepharose 4B, with anti-rat GAPD rabbit antibodies was digested with papain. The antigen was inaccessible to proteolysis under conditions employed.

Effect of specific antibodies on D-glyceraldehyde-3-phosphate dehydrogenase.

The inhibition of rat skeletal muscle glyceraldehyde-3-phosphate dehydrogenase by specific antibodies produced in rabbits has been studied. The results suggest that no influence on the enzyme active site is caused by the interaction with antibody, the inhibition being due entirely to the restricted accessibility for substrates of a part of dehydrogenase molecules included in the immune precipitate. Soluble complexes of the enzyme with monovalent Fab antibody fragments retain full catalytic activity.