Dale J W
Antonie Van Leeuwenhoek. 1975;41(1):59-68. doi: 10.1007/BF02565036.
The production of beta-lactamase (penicillin/cephalosporin beta-lactam amidohydrolase, E.C.3.5.2.6) was found to be inducible in a clinically isolated strain of Escherichia coli. This is the first report of an inducible beta-lactamase in E. coli. The optimal concentration of inducer was 400 mug/ml of ml of benzylpenicillin, or 800 mug/ml of 6-aminopenicillanic acid. About fiftyfold induction was achieved. Maximum induction took ninety minutes from the time of adding the inducer. Induction was abolished by the presence of chloramphenicol(10 mug/ml). The enzyme has a molecular wieght of 23,000, and is inhibited by rho-chloromercuribenzoate and by iodine. It is active against a wide range of substrates, including cephaloridine and cloxacillin.
在一株临床分离的大肠杆菌中发现β-内酰胺酶（青霉素/头孢菌素β-内酰胺酰胺水解酶，E.C.3.5.2.6）的产生是可诱导的。这是关于大肠杆菌中可诱导β-内酰胺酶的首次报道。诱导剂的最佳浓度为每毫升400微克苄青霉素，或每毫升800微克6-氨基青霉烷酸。实现了约五十倍的诱导。从添加诱导剂时起，最大诱导作用需90分钟。氯霉素（10微克/毫升）的存在可消除诱导作用。该酶的分子量为23000，受对氯汞苯甲酸和碘抑制。它对多种底物具有活性，包括头孢利定和氯唑西林。
