Abstract
The penicillin-binding proteins (PBPs) of Haemophilus influenzae were studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Eight major PBPs, ranging in molecular weights from 90,000 to 27,000, were detected. The pattern of molecular weights was different from that determined fro Escherichia coli or Pseudomonas aeruginosa. A study on the binding of several beta-lactam antibodies to the PBPs at their minimal inhibitory concentrations and at lower and higher concentrations revealed that all had highest affinity for PBP 2. Amdinocillin (mecillinam) was an exception; it had highest affinity for PBP 3. The morphological effects of several penicillins, cephalosporins, and amdinocillin on H. influenzae were similar to those reported for E. coli.