Beta-Lactamase Activity in Strains of Bacteroides melaninogenicus and Bacteroides oralis
AUTOR(ES)
Salyers, A. A.
RESUMO
β-Lactamase from strains of Bacteroides melaninogenicus and Bacteroides oralis hydrolyzed penicillin more rapidly than ampicillin or carbenicillin. Cephalothin and a chromogenic cephalosporin (87/312) were also hydrolyzed by the enzyme. Activity was found only in β-lactam-resistant strains, but there was considerable variation in activity among strains having the same minimal inhibitory concentrations of antibiotic. β-Lactamase activity was cell bound and appeared to be tightly associated with the cell envelope since detergents were required to elute this activity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=351933Documentos Relacionados
- Activity of cefoperazone and two beta-lactamase inhibitors, sulbactam and clavulanic acid, against Bacteroides spp. correlated with beta-lactamase production.
- Formation of Beta-Lactamase in Bacteroides fragilis: Cell-Bound and Extracellular Activity
- Role of Bacteroides bivius beta-lactamase in beta-lactam susceptibility.
- Purification and properties of beta-lactamase from Bacteroides fragilis.
- Activity of beta-lactamase produced by Bacteroides fragilis against newly introduced cephalosporins.