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Biomedical subjects

N F Iankina

Publications and source records attributed to N F Iankina.

8 recordsLinked to original sources

[The production of specific immunoenzyme conjugates to human immunoglobulins by the glutaraldehyde method].

The results of studies aimed at obtaining class-specific conjugates to human immunoglobulins to be used in the enzyme immunoassay (EIA) are presented. At the first stage of the studies purified IgA, IgM and IgG preparations were obtained. These preparations were used for obtaining immunologically active immunosorbents on the basis of bromocyanic Sepharose. Specific antibodies to human IgA, IgM and IgG were isolated from animal sera by the method of affinity chromatography. These antibodies were conjugated with peroxidase by the glutaraldehyde method. The specific activity of the conjugates were determined in EIA. The results thus obtained revealed that all preparations exhibited high specific activity and gave no cross reactions with immunoglobulins of other classes.

Antibody Specificity

[The development of an immunoenzyme method for determining human secretory IgA].

The results of the work on the development of an enzyme immunoassay (EIA) system for the determination of secretory IgA (S-IgA) are presented. A first, S-IgA was isolated from human colostrum and used as the basis for obtaining biologically active immunosorbent; then antibodies to S-IgA were isolated and the specific conjugate was obtained. The determination of S-IgA was carried out by the method of sandwich EIA. The newly developed EIA system permitted the determination of S-IgA only, giving no positive reactions with serum immunoglobulins. The data thus obtained make it possible to regard this assay system as specific, sensitive and suitable for further trials.

Antibody Specificity

[Use of an affinity chromatography method for isolating monospecific Salmonella antibodies].

Obtaining antibodies to individual components of Salmonella antigenic complex is highly important for investigations aimed at the study of the antigenic structure of bacteria, their serological identification and the development of diagnostic preparations. The method of obtaining antibodies by the oxidation of Salmonella antigens with sodium periodate and creating immunosorbents based on these antibodies with subsequent affinity chromatography has been developed. Monospecific antibodies thus obtained (O2, O4, O9) have been studied and used as monospecific preparations in the agglutination test, the immunofluorescence test and the immunosorbent assay. The development of methods for stabilizing these preparations, thus ensuring their wide practical use, may be of interest.

Agglutination Tests

[The development of methods for obtaining monospecific ingredients for immunoenzyme analysis].

The methods of the modification of Salmonella O- and H-antigens and the preparation of biologically active sorbents on their basis have been developed. The use of these sorbents has permitted the isolation of affinity antibodies with strictly defined specific activity. The work shows the possibility of the successful use of carriers obtained on the basis of porous glass, chemically modified by acrylic copolymers containing activated carboxylic groups, and intended for the immobilization of antigens of both protein and carbohydrate nature.

Animals

[Isolation of monospecific Salmonella anti-O-4 antibodies by affinity chromatography and their use in immunoenzyme reactions].

An immunosorbent with Salmonella typhimurium 1021 O-antigen has been obtained on the basis of polymer-modified porous glass. Binding has been effected due to the presence of NH2-groups on the carrier and aldehyde groupings on O-antigen previously oxidized with sodium periodate. Specific anti-O-4 antibodies have been isolated with the use of this immunosorbent, and on the basis of these antibodies peroxidase conjugates have been obtained. This preparation has made it possible to establish the parameters of EIA for the detection of Salmonella O-4 antigens in the assay involving the use of the sandwich technique. The method has proved to be sufficiently simple, sensitive and specific. It is recommended for the detection of Salmonella O-4 antigen in biological fluids.

Animals

[Synthesis of a repeating unit and the dimer of the repeating unit of the major chain of Shigella flexneri O-antigen polysaccharide].

Methyl glycoside of the tetrasaccharide GlcNAc(beta 1-2)Rha(alpha 1-2)Rha(alpha 1-3)Rha, which represents a repeating unit of the basic chain of Shigella flexneri O-antigenic polysaccharides, was synthesized using acylated monosaccharide synthons. A dimer of the repeating unit, octasaccharide [GlcNAc(beta 1-2)Rha(alpha 1-2) Rha(alpha 1-3)Rha(alpha 1-3)]2-OMe was obtained by TrClO4-catalyzed condensation of two tetrasaccharide blocks.

Antigens, Bacterial

[Rapid immunoenzyme analysis].

A variant of the immunoenzyme assay, reducing the duration of the assay procedure by 3 hours in comparison with the standard technique, is presented. This rapid variant is sufficiently sensitive and reproducible.

Antigens, Bacterial

[Development of a method of obtaining peroxidase conjugates with anti-immunoglobulin for immunoenzyme analysis].

The results of the successive stages of preparing peroxidase-labeled anti-immunoglobulins are presented. The schedules for the immunization of animals have been worked out with a view to prepare antisera to human gamma globulin and, subsequently, to isolate antibodies from them by different methods. The preparations obtained with the use of immunosorbent have proved to possess the highest serological activity. As the result of these investigations, a new method of binding, a modification of the glutaraldehyde method, has been proposed. The conjugates obtained by the proposed method are characterized by high serological activity, stability and good reproducibility.

Animals