Berenguer J, De Pedro M A, Vázquez D V
Eur J Biochem. 1982 Aug;126(1):155-9. doi: 10.1111/j.1432-1033.1982.tb06760.x.
This study deals with the interaction of nocardicin A with Escherichia coli penicillin-binding proteins. Competition experiments with two different isotopically labelled beta-lactams indicated that nocardicin A interacts with penicillin-binding proteins 1a, 1b, 2 and 4 in intact cells. Binding of nocardicin A to the penicillin-binding proteins was abolished, or greatly reduced, when the assays were carried out with purified cell envelopes. Important differences between the binding patterns of benzyl[14C]penicillin to intact cells and to purified cell envelopes were also observed. These results suggest that the interaction of beta-lactam antibiotics with their target proteins depends to a very great extent on the state of the cell envelope as a whole.
本研究探讨了诺卡菌素A与大肠杆菌青霉素结合蛋白的相互作用。用两种不同同位素标记的β-内酰胺进行的竞争实验表明，诺卡菌素A在完整细胞中与青霉素结合蛋白1a、1b、2和4相互作用。当用纯化的细胞包膜进行测定时，诺卡菌素A与青霉素结合蛋白的结合被消除或大大减少。还观察到苄基[14C]青霉素与完整细胞和纯化细胞包膜的结合模式存在重要差异。这些结果表明，β-内酰胺抗生素与其靶蛋白的相互作用在很大程度上取决于整个细胞包膜的状态。
