Farmer T, Reading C
Drugs. 1986;31 Suppl 3:70-8. doi: 10.2165/00003495-198600313-00015.
The beta-lactamases of Branhamella catarrhalis Ravasio and strain 1908 were readily inhibited by low concentrations of sulbactam, beta-halopenicillanic acids, MM 13902 and clavulanic acid. More detailed studies on the interaction of the Ravasio beta-lactamase with clavulanic acid demonstrated that the enzyme had high affinity for the inhibitor (Ki = 0.07 mumol/L) and was rapidly inhibited (t1/2 = 21 sec, kinhib. = 0.033/sec). Two types of enzyme-inhibitor complex were formed, a transiently stable species (t1/2 = 5.3 minutes at pH 7.3 and 37 degrees C) and a more stable species (t1/2 approximately equal to 2 hours at pH 7.3 and 37 degrees C). Irreversible inactivation of the enzyme was not achieved. Permeability studies on whole cells showed that beta-lactam antibiotics and beta-lactamase inhibitors readily penetrated the outer membrane of B. catarrhalis.
卡他布兰汉菌拉瓦西菌株和1908菌株的β-内酰胺酶很容易被低浓度的舒巴坦、β-卤代青霉烷酸、MM 13902和克拉维酸抑制。对拉瓦西β-内酰胺酶与克拉维酸相互作用的更详细研究表明，该酶对抑制剂具有高亲和力（Ki = 0.07 μmol/L），并且被迅速抑制（t1/2 = 21秒，kinhib. = 0.033/秒）。形成了两种类型的酶-抑制剂复合物，一种是短暂稳定的物种（在pH 7.3和37℃下t1/2 = 5.3分钟）和一种更稳定的物种（在pH 7.3和37℃下t1/2约等于2小时）。未实现酶的不可逆失活。对全细胞的通透性研究表明，β-内酰胺抗生素和β-内酰胺酶抑制剂很容易穿透卡他布兰汉菌的外膜。
