Both a penicillinase and a cephalosporinase were purified from a strain of (GN7647) resistant to β-lactam antibiotics. The penicillinase was identical to the type I penicillinase, mediated by Rms212 and R-TEM. The purified cephalosporinase, a typical chromosomally mediated enterobacterial β-lactamase, gave a single protein band on polyacrylamide gel electrophoresis and immunoelectrophoresis; the pI was 9·56 and its molecular weight was approximately 37000. It contained tryptophan but not cysteine. The specific activity was 374 units (mg protein) for the hydrolysis of cephaloridine, and the optimal pH was 8·5. Rabbit antisera raised against the purified cephalosporinase showed no cross-reaction in a neutralization test with cephalosporinases produced by other species of .


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