Georgopapadakou N H, Liu F Y
Antimicrob Agents Chemother. 1980 Jul;18(1):148-57. doi: 10.1128/AAC.18.1.148.
The penicilllin-binding proteins (PBPs) of several gram-positive and gram-negative bacteria have been examined. The results indicate that: (i) PBPs are membrane proteins with molecular weights ranging from 40,000 to 120,000. When extracted with Triton X-100 from sonicated cells, they appear to fall into two patterns: one found in rods and the other in spheres. A major difference is in the low-molecular-weight component, which is usually the major PBP in bacilli but a minor one in cocci. (ii) There is a wide variation in both the number and the amount of PBPs in different bacteria, and taxonomically related bacteria tend to have similar PBP patterns. These patterns often correlate with the affinity of PBPs for penicillin and other beta-lactam antibiotics. (iii) The low-molecular-weight component usually releases penicillin spontaneously with a half-life of 10 min or less. Most, but not all, PBPs release bound penicillin in the presence of neutral hydroxylamine (0.2 to 0.8 M).
已对几种革兰氏阳性菌和革兰氏阴性菌的青霉素结合蛋白（PBPs）进行了检测。结果表明：（i）PBPs是分子量在40,000至120,000之间的膜蛋白。用Triton X - 100从超声破碎的细胞中提取时，它们似乎呈现出两种模式：一种存在于杆菌中，另一种存在于球菌中。主要差异在于低分子量组分，它通常是杆菌中的主要PBP，但在球菌中是次要的。（ii）不同细菌中PBPs的数量和含量存在很大差异，并且分类学上相关的细菌往往具有相似的PBP模式。这些模式通常与PBPs对青霉素和其他β-内酰胺类抗生素的亲和力相关。（iii）低分子量组分通常会自发释放青霉素，半衰期为10分钟或更短。大多数（但不是全部）PBPs在中性羟胺（0.2至0.8M）存在下会释放结合的青霉素。
