1981 Volume 34 Issue 9 Pages 1164-1170
Cephalosporin β-lactamase (cephalosporinase; CSase) was purified from a strain of Pseudomonas aeruginosa resistant to β-lactam antibiotics. The purified enzyme preparation gave a single protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its molecular weight was about 34, 000. The specific activity was 49.7 μmoles/minute/mg of protein of the purified enzyme for the hydrolysis of cephaloridine. The optimal pH and optimal temperature were about 8.0 and 40°C, respectively. Its isoelectric point was 8.7. The enzyme activity was inhibited by iodine, some divalent ions, and some semisynthetic β-lactam antibiotics, including cephamycin derivatives such as moxalactam and YM09330. Mouse antiserum obtained against the purified enzyme showed no cross-reaction with other types of β-lactamase in neutralization test.
