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Biomedical subjects

T N Batalova

Publications and source records attributed to T N Batalova.

11 recordsLinked to original sources

[The level of immunoglobulins in the blood serum of guinea pigs with epicutaneous exposure to petroleum refinery products].

Blood serum IgG1, IgG2, IgA, and IgM were assayed by radial immunodiffusion after exposure of guinea pig skin to oil refinery products, mineral oil distillate D-11 (MOD) and furfurol (F), applied both separately and together. Application of MOD, F, and MOD + F subthreshold concentrations was found to be associated with a tendency to a reduction of IgG1 level; isolated applications of the agents in threshold concentrations involved statistically significant lowering of IgG1 (in exposure to MOD) and imbalanced levels of IgG1, IgG2, IgA, and IgM (in exposure to F). Combined application of both agents induced immunity shifts of other type as against isolated exposure.

Animals

[Isolation of monospecific antisera to guinea pig immunoglobulins].

The results of the production and analysis of monospecific rabbit antisera to guinea pig IgG1, IgG2, IgA and IgM are presented. Isolated immunoglobulins of different isotypes, as well as immune precipitates obtained by immunoelectrophoresis, were used for immunization. After adsorption antisera of each type there formed one precipitation line with guinea pig serum in immunoelectrophoresis, thus indicating that they contained antibodies to immunoglobulins of the definite isotype.

Animals

[IgD myeloma].

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Adult

[Immunochemical study of serum in the diagnosis of mu-chain disease].

An abnormal protein revealed in the serum of a patient with an unknown lymphoproliferative disorder proved to be micron-paraprotein: micron-heavy chain complexes of various molecular weight totally lacking light chains. The results of immunochemical analysis of this case are compared with the published data on micron-chain disease. The following immunochemical features typical for micron-chain disease were observed in this patient: anodal mobility of paraprotein, failure to reveal it by serum electrophoresis, that is, absence of M-gradient, and presence of Bence Jones protein, type x in the urine and the serum. The peculiarity of the case consists in a high tendency of free x-chains to form complexes, and therefore in their marked electrophoretic heterogeneity giving a false impresssion of the ability of micron-paraprotein to react with the anti-x serum, thus complicating the diagnosis. Possible causes of a defect in the IgM assembly are discussed.

Bence Jones Protein

[Subclasses of immunoglobulin G. I. Determination of subclasses of G-paraproteins by the method of tryptic splitting].

Subclasses of the G-paraproteins were examined by the method of tryptic splitting of the sera. The fragments were identified in the immunoelectrophoresis with the antisera detecting the IgG, Fab-, Fc- and Fc1-fragments. It was revealed that for the IgGI most typical was formation of the Fc1-fragment continuously detected along with the Fab- and Fc-fragments; for the IgG1--retention of a considerable amount of unsplit protein; for the IgG3--formation of the Fab- and Fc-fragments, for the IgG4-- of the Fab-fragment alone. Analysis of 96 sera of the patients suffering from G-myeloma showed that 69 were referred to the IgGl, 19 - to the IgG2, 5 - to the IgG3, and 3 - to the IgG4. The method tested permitted successful identification of subclasses of the G-paraproteins, this serving as the necessary prerequisite for the choice of antigens and sorbents in the preparation of the subclass-specific antisera.

Catalysis

[Light chain typing of paraproteins and Bence-Jones proteins by immunoelectrophoresis].

Light chain types of paraproteins G (76), A (28) and D (5), monoclonal macroglobulins (14) and Bence-Jones proteins (11) were determined by immunoelectrophoretic analysis using monospecific antisera to surface (accessible) and nonaccessible determinants of light chains. The types of the G and A paraproteins were determined in the whole sera; D paraproteins and monoclonal macroglobulins were purified before typing. No precipitation occurred with antisera to light chains in 6 out of 28 A paraproteins. In these cases the inhibition of the IgG precipitation with either the anti-kappa or anti-lambda sera allowed to determine the paraprotein type. The kappa:lambda ratio was established for paraproteins of various classes: 1.7 for paraproteins G, 1.0 for paraproteins A, 2.5 for monoclonal macroglobulins and 0.83 for Bence-Jones proteins. All the D paraproteins investigated were of the lambds-type.

Bence Jones Protein