SUMMARYA method is described for the preparation, on a laboratory scale, of staphylococcal alpha toxin having a purity of about 70% and in a yield of 40 %. The method entails ammonium sulphate fractionation followed by curtain electrophoresis. The toxin so obtained contains two impurities, one of which can be removed electrophoretically, and the other ultracentrifugally. The toxin itself is a protein of molecular weight 44,000.
Seventeen bacterial toxins were examined for capacity (i) to disrupt rabbit leukocyte lysosomes as indicated by decrease in turbidity of lysosomal suspensions, and (ii) to alter rabbit liver lysosomes as measured by release of ,B-glucuronidase and acid phosphatase. Staphylococcal a-toxin, Clostridium perfringens a-toxin, and streptolysins 0 and S affected lysosomes in both systems. Staphylococcal 3-toxin, leucocidin and enterotoxin, Shiga neurotoxin, Serratia endotoxin, diphtheria toxin, tetanus neurotoxin, C. botulinum type A toxin, and C. perfringens e-toxin were not active in either system. Staphylococcal s-toxin, C. histolyticum collagenase, crude C. perfringens A-toxin, and crude anthrax toxin caused lysosomal damage in only one of the test systems. There is a substantial correlation between the hemolytic property of a toxin and its capacity to disrupt lysosomes, lending support to the concept that erythrocytes and lysosomes are bounded by similar membranes.
Protoplasts of Bacillus itoegateriiu Sarcina littea, and Streptococc us pyo genes, anid spheroplasts of Escherichia coli were lysed by stap)hylococcal a-toxin, whereas sptheroplasts of Vibrio ntietschnikovii aiid V. cootutia were Iiot. In the spectrum of its lytic actioli, streptolysin S qualitatively resenmbled staphylococcal a-toxin except for failure to lyse S. pylogenes protoplasts. In contrast to the two foregoing agents, streptolysin 0 did not lyse protoplasts and spheroplasts. The observations are interprete(d in relation to similarities and differeinces in lipid comiiposition of bacterial and manmmaliain cell nmembranes.
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