Abstract
Summary
It was possible to demonstrate the existence of a potent reduced diphosphopyridine nucleotide oxidase in all Neisseria. This enzyme and alcohol dehydrogenase were increased in relative penicillin-resistant isolates of N. gonorrhoeae. Another potent enzyme found was diphosphopyridine nucleotide-linked lactic dehydrogenase. Some organisms contained much less LDH and DPNH oxidase than N. gonorrhoeae isolates. Reduced triphosphopyridine nucleotide oxidase was present only in small quantities in all organisms investigated. An acetate oxidizing enzyme system was present in large quantities in E. coli and S. aureus, in small quantities in N. sicca and TV. catarrhalis, and in traces in a few isolates of N. gonorrhoeae. The system was absent from N. meningitidis. For the above enzymes, the Thunberg technic with tetrazolium salt as the electron acceptor was employed. All Neisseria contained a cyanide sensitive, aerobic cysteine oxidase and a cysteine desulfhydrase. It is hoped that the present investigation will aid in identification and classification of Neisseria.
These results were obtained with old stock cultures of N. gonorrhoeae. When a large number of fresh isolates was assayed only partial correlation between penicillin resistance and enzyme activity was observed.
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