Farrar W E, O'Dell N M
Antimicrob Agents Chemother. 1974 Nov;6(5):625-9. doi: 10.1128/AAC.6.5.625.
The specific activity, substrate profile, response to inhibitors, inducibility, and cellular localization of the beta-lactamase produced by an ampicillin-resistant strain of Haemophilus influenzae type B were investigated. In these properties the enzyme resembles beta-lactamases produced by other gram-negative bacilli more closely than those produced by gram-positive organisms. It is quite similar to an enzyme found in strains of Klebsiella pneumoniae, and differs significantly from those described in other gram-negative bacilli. Comparison of the substrate profile with the minimal inhibitory concentrations of various beta-lactamase antibiotics suggests that the beta-lactamase plays an important role in the antibiotic resistance of this organism.
对一株B型流感嗜血杆菌氨苄西林耐药菌株产生的β-内酰胺酶的比活性、底物谱、对抑制剂的反应、诱导性及细胞定位进行了研究。在这些特性方面，该酶与其他革兰氏阴性杆菌产生的β-内酰胺酶更为相似，而与革兰氏阳性菌产生的β-内酰胺酶差异较大。它与肺炎克雷伯菌菌株中发现的一种酶非常相似，与其他革兰氏阴性杆菌中描述的酶有显著差异。将底物谱与各种β-内酰胺酶抗生素的最低抑菌浓度进行比较表明，β-内酰胺酶在该菌的抗生素耐药性中起重要作用。
