[An evaluation of the protective activity of a multicomponent vaccine made from opportunistic microorganisms in the oral method of immunization in a model of local staphylococcal infection].

The protective activity of a multicomponent vaccine against S. aureus, prepared from Staphylococcus, Klebsiella, Proteus and Escherichia coli antigens, intended for oral administration, has been studied on the model of a local staphylococcal infection. The study has revealed that the vaccine, when administered orally to mice, prevents the development of gangrene in the paw, the death of the animals, and essentially decreases the local focus of infection.

[The antigenic activity of vaccines made from opportunistic microorganisms in an experiment to immunize animals by oral and combined methods].

The results of the study of the antigenic activity of multicomponent vaccine consisting of staphylococcal, Klebsiella, Proteus, Escherichia coli antigens and staphylococcal monovaccine, introduced into rabbits and guinea pigs by different routes, are presented. As shown in this study, the multicomponent vaccine introduced orally in 5 administrations stimulated the production of antibodies to all components, but the intensity of antibody formation to each of them was different. Antibodies to E.

[The specific activity of a multicomponent vaccine made from the antigens of opportunistic microorganisms].

Multicomponent vaccine prepared from the antigens of 4 representatives of opportunistic microflora possesses high specific activity. The passive hemagglutination (PHA) test with the use of associated diagnosticum showed that antibody titers in the sera of immunized rabbits increased 10- to 10(4)-fold in comparison with the titers observed prior to immunization. The PHA test with the use of the antigens contained in the vaccine revealed the accumulation of antibodies to each of the 4 components of the preparation in the blood sera of immunized rabbits.

[Isolation and characteristics of new restriction endonucleases from Haemophilus influenzae].

Various strains of Haemophilus influenzae have been examined for the presence of site-specific endonuclease activities, and eleven restriction endonucleases have been isolated from seven strains. For all the endonucleases recognition sequences were determined, for three of them cleavage sites being identified. The enzymes proved to be isoschizomers of known endonucleases, viz.

[The method of isolation of Sau 6782-type methylases].

Heterogeneous profile of methylases was found in S. aureus 6782 strain. A procedure was developed for isolation of individual methylases from Sau 6782 free of Sau 6782 restrictases and unspecific nucleases by means of hydrophobic chromatography on phenyl-Sepharose.

[Design of a nutrient medium for bacteria of the genus Haemophilus--producers of restriction endonucleases].

A culture medium for the cultivation of hemophilic bacteria, containing acidic casein hydrolysate, aminopeptide and fodder yeast extract, has been proposed. The growth-stimulating properties of this medium have been studied on 5 strains producing restrictases differing in their specificity. In growing these producer strains in a model ANKUM-2 fermenter with the supply of carbohydrate substrates (glucose, sucrose, glycerin) the yield of biomass, considered to be high for hemophilic bacteria (10-14 g of humid substance from 1 liter of the medium), has been achieved.

[Activity of restriction endonuclease Sso II in Escherichia coli strains transformed by Shigella sonnei 47 plasmids].

The inverse dependence of activity of restriction endonuclease SsoII preparations on the number of low molecular mass plasmids of Shigella sonnei transforming Escherichia coli recipient cells producing the enzyme has been shown. Escherichia coli strain producing efficiently one of two Shigella sonnei 47 restriction endonucleases SsoII has been isolated. The producer strain harbours two of the nine Shigella sonnei 47 plasmids.

[Purification and substrate specificity of BcmI restriction endonuclease].

A strain producing the new specific restriction endonuclease BcmI has been found in the Bacillus generum. The enzyme has been purified by chromatography on the blue sepharose, phosphocellulose PII, heparin sepharose. The analogous purification has been obtained when the blue sepharose has been substituted for the orange sepharose, the home produced sorbent.

[Restriction endonuclease Sau 6782].

Data are described on identification, isolation and purification of restricting endonuclease Sau 6782 as well as on estimation of the enzyme recognition site. Conditions were developed for growing of Staphylococcus aureus 6782 strain, which enabled to produce a maximal yield of the restricting activity containing minimal level of nucleases. The procedure for isolation and purification of restrictase Sau 6782 involved affinity chromatography on Blue Sepharose and cation exchange chromatography on phosphocellulose PII.