SUMMARY: Antisera to the penicillinases of strains 749 and 6346 were prepared, and the neutralization of enzymie activity by homologous and heterologous antisera was studied. Antisera to 749 penicillinase had, as expected, greater neutralizing power against 749 penicillinase than against 6346 penicillinase. A 6346 antiserum, however, neutralized the heterologous enzyme more effectively than the homologous enzyme, and was also more effective in precipitating heterologous than homologous enzymic activity. The penicillinases of , unlike those of , could not be adsorbed on glass, but could be partially purified by calcium phosphate gel-adsorption. There was no cross-reaction, as measured by enzyme neutralization, between the penicillinases of and that of 569. Materials other than penicillinase in the enzyme preparations used did not interfere with the neutralization reactions between penicillinases and their antisera. The basal penicillinase produced by 749 had the same neutralization curve, with a homologous antiserum, as did the induced enzyme.


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