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SUMMARY: Exocellular penicillinases from strains 569 and 5/B of BuciZZus cereus gave almost identical activity-neutralization curves when titrated with antisera prepared against the enzyme from either strain ; but were easily distinguishable by differences in their neutralization reaction with an anti-569 penicillinase serum previously partially absorbed with either the 5/B or the 569 enzyme. By contrast, no differences in neutralization reaction were detected between basal and induced penicillinase from strain 569 and the constitutive penicillinase from strain 569/H (a mutant derived from strain 569), when treated with samples of the anti-569 penicillinase serum, previously partially absorbed with each penicillinase preparation separately. Strain 569 was not found to produce any substance in significant quantities capable of combining with anti-penicillinase neutralizing antibodies other than penicillinase itself. Although it has been known for many years that enzymically active proteins may evoke the production of precipitating and neutralizing antibodies in animals, relatively little systematic work has been done on the neutralization reaction, Toxin neutralization by specific antitoxin has of course been investi- gated in detail, but, except in those cases where the toxin is itself enzymically active and has a well-defined substrate, such studies suffer from the dis- advantages of cumbrous and inaccurate in vivo titration of biological activity. In those instances where an enzyme stimulates the formation of antibodies which will neutralize-to a greater or lesser extent-enzymic activity, the antigen-antibody reaction can be studied quantitatively at relatively low concentrations of the reagents from an aspect which is distinct from the precipitation reaction and can thus be expected to shed new light on the character of the specific combination. Some of the possibilities offered by such studies of enzyme-antibody reactions have been outlined in a stimulating article by Cinader (1953); and the subject has been reviewed by Sevag (1951). Quite apart from its general immunological interest, the pioneer work of Cohn & Torriani (1952,1953) on the properties of induced P-galactosidase and the related protein Pz in Escherichia coli has shown clearly the advantages to be gained by the application of immunological methods to the study of induced enzyme synthesis in micro-organisms. Housewright & Henry (1947) showed that penicillinase from Bacillus cereus, strain 569 can evoke the produc- tion of penicillinase-inhibiting antibodies in rabbits. The present work was begun as an immunological analysis of penicillinase induction, analogous to that carried out by Cohn & Torriani on 16-galactosidase formation in Escherichia

journal of general microbiology/journal of general microbiology

An Immunological Study of the Constitutive and the Penicillin-induced Penicillinases of Bacillus cereus, Based on Specific Enzyme Neutralization by Antibody