NDLI: Properties of a new penicillinase type produced by Bacteroides fragilis.

Content Provider	PubMed Central
Author	Sato, K. Matsuura, Y. Inoue, M. Mitsuhashi, S.
Abstract	A highly penicillin-resistant strain of Bacteroides fragilis, strain GN11499, was found among 80 clinical isolates of the B.fragilis group and appears to produce a new type of penicillinase. Penicillinase activity was detected in crude extracts and had a specific activity of 0.25 U/mg of protein. About 20% of the enzyme was released into the surrounding medium during growth. The enzyme hydrolyzed ampicillin and cloxacillin more rapidly than it did penicillin G, carbenicillin, and cephaloridine. Relative rates in a crude extract with penicillin G as 100 were ampicillin, 357; carbenicillin, 57; cloxacillin, 271; and cephaloridine, 71. Enzyme activity was inhibited by clavulanic acid, CP-45, 899, N-formimidoyl thienamycin, cefoxitin, moxalactam, and p-chloromercuribenzoate. The enzyme had a molecular weight of approximately 41,500 and an isoelectric point of 6.9. Penicillinase production and tetracycline resistance were transferred from B.fragilis GN11499 to two susceptible strains of B.fragilis and Bacteroides vulgatus by filter mating.
Starting Page	579
File Format	PDF
ISSN	10986596
e-ISSN	10986596
Journal	Antimicrobial Agents and Chemotherapy
Issue Number	4
Volume Number	22
Language	English
Publisher Date	1982-10-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Pharmacology Pharmacology (medical)

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Properties of a new penicillinase type produced by Bacteroides fragilis.