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Biomedical subjects

E A Shkurina

Publications and source records attributed to E A Shkurina.

7 recordsLinked to original sources
PubMed1991

[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↗
PubMed1990

[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↗
PubMed1989

[Antigen-antibody complex dissociation in affinity chromatography].

Different methods of the elution of antibodies from an immunosorbent column have been studied, the serological activity and affinity of eluted antibodies have been evaluated in the enzyme immunoassay. The activity of conjugates (peroxidase-labeled antibodies) has been shown to depend not only on the serological activity and affinity of antibodies, but also on the method of binding antibodies with the enzyme.

Adsorption↗
PubMed1987

[Determination of the binding constants of immune serum antibodies to human IgG].

The possibility of using two variants of the enzyme-linked fluorescent cofactor immunoassay for the determination of antibody binding constants has been demonstrated. The determination of binding constants for antibodies isolated by affinity chromatography techniques has been carried out. These techniques permit the isolation of fractions, differing in their affinity by 5-10 times, from the whole population of antibodies.

Adenosine Triphosphate↗
PubMedDate not supplied

[The comparative characteristics of the peroxidase conjugates used in Soviet immunoenzyme test systems for detecting HIV antibodies].

Five lots of peroxidase conjugates were studied in enzyme immunoassay systems "Recombinant-HIV" and "Peptoscreen-2" for detection of antibody to HIV. The conjugates differed from each other by the source of generation and methods of preparation. The conjugates were studied in biochemical tests and ELISA. When panels of sera from HIV-infected children and adults were employed, the advantages of using the anti-immunoglobulin conjugate over protein A-peroxidase conjugate were demonstrated, as the former increased the sensitivity of the test systems to HIV antibody detection.

Evaluation Studies as Topic↗
PubMedDate not supplied

[The effect of detergents on the immunological activity of the antigens of Neisseria meningitidis serogroup B[].

The complex study of the influence of detergents of different classes and aluminum hydroxide, a traditional adjuvant, on the immunological activity of individual N. meningitidis antigens (outer membrane proteins, polysaccharide B) and the complex preparation containing all these antigens revealed that changes in the antigenic and immunogenic properties of the antigens under study depended on the degree of their purification and the character of modifying substances. Aluminum hydroxide proved to be the most active adjuvant: it stimulated immune response to both outer membrane proteins and antigens of the protein-polysaccharide complex, while decreasing the antigenicity of outer membrane proteins and polysaccharide. Detergents increased the antigenicity of outer membrane proteins, both purified and, to a lesser extent, contained in the complex; still the immune response only to the purified preparation could be stimulated.

Aluminum Hydroxide↗