Barbour A G
Antimicrob Agents Chemother. 1981 Feb;19(2):316-22. doi: 10.1128/AAC.19.2.316.
The properties of penicillin-binding proteins (PBPs) of Neisseria gonorrhoeae were studied by comparing PBPs of clinical isolates of different penicillin susceptibility and by putting various beta-lactam antibiotics in competition with radioactive penicillin for PBP binding. Apparent molecular weights of the three major PBPs found were 87,000 (PBP 1), 59,000 (PBP 2), and 44,000 (PBP 3). Relative penicillin resistance was associated with decreased binding to PBP 2 and, to a lesser extent, to PBP 1. Cephaloridine and benzylpenicillin, which produced spheroplasts at minimal inhibitory concentrations, bound to all three PBPs. In contrast, antibiotics which produced a majority of enlarged but apparently intact cells bound only to PBP 2 (mecillinam) or to PBPs 2 and 3 (cephalexin) at their minimal inhibitory concentrations.
通过比较不同青霉素敏感性临床分离株的青霉素结合蛋白（PBPs），并使各种β-内酰胺抗生素与放射性青霉素竞争PBP结合，研究了淋病奈瑟菌青霉素结合蛋白的特性。发现的三种主要PBPs的表观分子量分别为87,000（PBP 1）、59,000（PBP 2）和44,000（PBP 3）。相对青霉素耐药性与PBP 2结合减少有关，在较小程度上与PBP 1结合减少有关。在最低抑菌浓度下产生原生质球的头孢菌素和苄青霉素与所有三种PBPs结合。相比之下，在最低抑菌浓度下产生大多数细胞增大但明显完整的抗生素仅与PBP 2（美西林）或与PBP 2和3（头孢氨苄）结合。
