[Molecular structure and immunochemical properties of highly purified hemagglutinin from Clostridium botulinum type A].

A procedure for isolation of highly purified hemagglutinin from a toxic complex of culture filtrates of Cl. botulinum type A is described. This procedure includes precipitation with (NH4)2SO4, chromatography on Sephadex G-100, G-200 and DEAE-cellulose, specific adsorption on human erythrocytes and affinity chromatography.

[Protective properties of theta-hemolysin obtained by affinity chromatography].

The data on the study of the protective activity of theta hemolysin and Cl. perfringens lecithinase preparations and the corresponding antitoxic sera obtained by indirect immune affinity chromatography are presented. Experiments in mice and guinea pigs indicate that the injection of antihemolytic serum and immunization with anatheta hemolysin ensures the protection of the animals from theta toxin.

[Immunogenic properties of Clostridium perfringens type A anatheta-hemolysin].

Guinea-pigs were immunized with anatheta-hemolysin preparations adsorbed on aluminum hydroxide, as well as with the mixture of anatheta-hemolysin and type A Cl. perfringens toxoid, purified and concentrated. Anatheta hemolysin preparations were obtained with the use of homogeneous theta hemolysin, as well theta hemolysin of various purification degrees.

[Isolation of the theta-hemolysin of Cl. perfringens].

Teta-hemolysine was purified from Cl. perfringens strain BP6K 28 as follows: reprecipitation in the isoelectric point of the enzyme with 2 N H2SO4 containing 15% NaCl, DEAE cellulose chromatography, gel filtration on Sephadex G-100-G75 or Bio Gel P-60--P-100, rechromatography on DEAE-Sephadex A-50 and affinity chromatography. The biological activity of homogenous teta-hemolysine, estimated by complete hemolysis of human erythrocytes, exceeded 100, 000 theta E over mg protein but the enzyme was highly labile.