Foweraker J E, Hawkey P M, Heritage J, Van Landuyt H W
Department of Microbiology, University of Leeds, United Kingdom.
Antimicrob Agents Chemother. 1990 Aug;34(8):1501-4. doi: 10.1128/AAC.34.8.1501.
A novel beta-lactamase activity which confers resistance to expanded-spectrum cephalosporins and penicillins has been found in strain IC 5/21 of Capnocytophaga spp. Enzyme activity migrated at a molecular size of 38,000 daltons and at an isoelectric point of 3.6, with a minor band at 4.1. Kinetic studies suggested that it belonged to Richmond and Sykes beta-lactamase class 1c. Isoelectric focusing could be achieved only if a nonionic detergent was added to the gel, suggesting the presence of a hydrophobic enzyme akin to a membrane-bound beta-lactamase of gram-positive bacteria. The location of the gene coding for this beta-lactamase is not yet known.
在二氧化碳嗜纤维菌属菌株IC 5/21中发现了一种新的β-内酰胺酶活性,该活性赋予了对广谱头孢菌素和青霉素的抗性。酶活性在分子大小为38,000道尔顿、等电点为3.6处迁移,在4.1处有一条次要条带。动力学研究表明它属于里士满和赛克斯β-内酰胺酶1c类。只有在向凝胶中加入非离子去污剂时才能实现等电聚焦,这表明存在一种类似于革兰氏阳性细菌膜结合β-内酰胺酶的疏水酶。编码这种β-内酰胺酶的基因位置尚不清楚。