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Biomedical subjects

M L Beĭlbaeva

Publications and source records attributed to M L Beĭlbaeva.

12 recordsLinked to original sources
PubMed1991

[The use of the aggregate hemagglutination reaction and immunoenzyme analysis in determining staphylococcal enterotoxin type D].

Type D purified staphylococcal enterotoxin and anti-enterotoxic serum to it were prepared. IgG isolated from the anti-enterotoxic serum by the affinity chromatography method was used to improve the specificity and sensitivity of the aggregate hemagglutination test (AHAT) and enzyme immunoassay (EIA). The developed AHAT and EIA variants intended for the indication of type D staphylococcal enterotoxin are characterized by a high resolution ability and strict specificity. The suggested methods are simple and may be used for the rapid diagnosis of staphylococcal toxin infections.

Enterotoxins↗
PubMed1991

[A simple method of purifying staphylococcal alpha-toxin and a study of its properties].

The simple method is proposed for isolation and purification of staphylococcal alpha-toxin that permits one to obtain the homogeneous toxic protein with high activity. The time necessary for maximal toxin production at cultivation has been defined. The thermostability and interferonogenic characteristics of the obtained alpha-toxin were studied.

Bacterial Toxins↗
PubMed1989

[Immunobiological properties of staphylococcal enterotoxins type A, B, C, D and E].

Comparative study of mitogenic and interferonogenic properties of staphylococcal enterotoxins of different serotypes is done. It is revealed that preparations of enterotoxins are polyclonal mitogens and have interferon-inducing activity. It is stated that enterotoxin of D type has the highest mitogenic activity, which is shown by interferon-inducing activity of A type toxin.

Antigens↗
PubMed1989

[Staphylococcal enterotoxin type E: isolation, purification, identification].

Homogeneous protein of staphylococcal enterotoxin type E has been isolated. The technique of isolation, permitting 48% yield of active material, includes concentration by ammonium sulfate precipitation, ion exchange chromatography on DEAE-cellulose and gel-filtration on sephacryl S-200. The molecular mass of the isolated protein is 32 Kd. Antigenic affinity of staphylococcal toxins types A and E has been established by immunochemical analysis.

Chromatography, Ion Exchange↗
PubMed1987

[Staphylococcal enterotoxin type D: isolation, purification, identification].

The three step scheme of isolation and purification of staphylococcal type D enterotoxin was elaborated to obtain the homogeneous protein. The scheme includes protein concentration by (NH4)2SO4 saturation and subsequent fractionation on DEAE-cellulose and Sephacryl S-200. The yield of homogeneous protein is 25.5%. The molecular mass of the 29,600 D protein was identified by electrophoresis in polyacrylamide gel in the presence of SDS. The enterotoxic dose for staphylococcal type D enterotoxin is 5 mkg per kg of body mass as identified in experiments with cats. Immunological identity of the obtained protein was established to the commercial preparation of staphylococcal enterotoxin D produced by "Serva".

Chromatography, Gel↗
PubMed1980

[Comparative immunochemical and immunoallergologic characteristics of staphylococci varying in pathogenicity. I. Immunochemical characteristics of the antigenic composition of S. aureus and S. epidermidis].

Chemical extracts and fractions prepared from pathogenic and nonpathogenic staphylococcal strains were studied with immunodiffusion. Antigens were detected reacting with both homologous and heterologous antisera against the intact coccal cells. The allergens obtained by acidic and alkaline extraction were highly active antigens. The preparation of S. epidermidis obtained by the method of Ando-Verzhikovsky had the lowest antigen level.

Allergens↗
PubMed1978

[Antigenic characteristics and various biological properties of glycoprotein from Neisseria meningitidis of serological group A].

It was shown that the antigen determining the group specificity of meningococcus belonging to serological group A was of mixed polysaccharide-protein nature. Carbohydrate component is responsible for the interaction with the group-specific antibodies in this antigen. Glycoprotein can be isolated both from the cells and from the culture fluid where it passes during the N. meningitidis cultivation in fluid nutrient medium. The described antigen possesses no properties of endotoxin.

Antigens, Bacterial↗