Summary: Four penicillin-binding proteins (PBPs) were observed in the soluble fraction of CB13, and designated PBP S1 (mol. wt 60000), PBP S2 (55000), PBP S3 (45000) and PBP S4 (40000). CB15, an independent isolate, possessed similar soluble PBPs, but not PBP S2. These soluble PBPs could be observed even when a cell suspension was directly reacted with [C]penicillin G. Two of the soluble PBPs, S1 and S2, released half their bound [C]penicillin G during a 10 min incubation, indicating that these PBPs have penicillinase-like activity. PBP S2 was very thermolabile and lost its penicillin-binding activity after incubation at 40 °C for 10 min. Mecillinam did not show selective binding to any of the soluble PBPs or to PBPs in the cell envelope.


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