[A new immunosorbent for purifying interferon].
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Animals↗
Biomedical subjects
O B Kleeva
Publications and source records attributed to O B Kleeva.
[Development of an immunoenzyme test system for determining the antigens of feed yeasts].
An enzyme immunoassay (EIA) system for the detection of fodder yeast antigens in the air of production areas at fodder protein producing plants has been developed. The method has proved to be highly sensitive and specific and shows advantages in comparison with the nonspecific method of low sensitivity, currently used at such plants. The sensitivity of solid-phase EIA techniques is 0.001 micrograms/ml (for protein) or 10(2)-10(3) cells/ml, and 10 ng/ml for soluble antigen. No cross reactions with bakers' yeast antigen have been observed.
Air Pollutants, Occupational↗
[Development of an immunoenzyme test system for detecting antibodies to commercial strains of feed yeasts].
ELISA as a specific and highly sensitive test system was used for the examination of large groups of workers employed in the production of fodder protein to detect antibodies to the production strains of fodder yeast. The results yielded by ELISA correlated well with those obtained by the serological luminescent techniques, but antibody titers determined by means of ELISA are 10-20 times higher.
Animal Feed↗
[An immunosorbent for interferon purification].
Immunoaffinity chromatography was shown to be the method achieving the most complete elimination of antigenic admixtures from leukocyte interferon preparations without the loss of the preparation activity. An affinity sorbent has been developed on the basis of covalently linked polyvinyl alcohol (PVA). The immobilization of the antigen-specific rabbit globulin in the preparation of the sorbent is achieved by reaction of protein amino groups with the activated matrix. The proposed sorbent achieved the elimination of the antigenic admixtures from interferon preparations as effectively as those prepared on the basis of sepharose 4B, the productivity of the purification process being at least 5 times higher. The proposed sorbent is stable at the limit values of rH, is not destroyed by detergents, is sterilized in the process of preparation. Owing to the strong linkage of the immobilized immunoglobulin with the PVA-carrier, immunoaffinity chromatography on this sorbent does not involve contamination of the preparations with rabbit globulin allergenic for man. The combination of a large pore structure, wetting ability, stiffness, mechanical and chemical stability allows the proposed sorbent to be recommended for use in modern large-scale biotechnological production.
Animals↗