Salyers A A, Wong J, Wilkins T D
Antimicrob Agents Chemother. 1977 Jan;11(1):142-6. doi: 10.1128/AAC.11.1.142.
beta-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 beta-lactam-resistant strains, but there was considerable variation in activity among strains having the same minimal inhibitory concentrations of antibiotic. beta-Lactamase activity was cell bound and appeared to be tightly associated with the cell envelope since detergents were required to elute this activity.
产黑色素拟杆菌和口腔拟杆菌菌株产生的β-内酰胺酶对青霉素的水解速度比对氨苄西林或羧苄西林更快。头孢噻吩和一种显色头孢菌素(87/312)也被该酶水解。仅在对β-内酰胺耐药的菌株中发现有活性,但在具有相同抗生素最低抑菌浓度的菌株中,活性存在相当大的差异。β-内酰胺酶活性与细胞结合,似乎与细胞膜紧密相关,因为需要用去污剂洗脱这种活性。