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Preliminary studies on beta-lactamases from aztreonam-resistant Enterobacter cloacae


, : Preliminary studies on beta-lactamases from aztreonam-resistant Enterobacter cloacae. Zhongguo Yaolixue Yu Dulixue Zazhi 8(4): 297-300

The high level beta-lactamases producing from 4 strains of aztreonam (Azt)-resistant Enterobacter cloacae (RAzt; minimal inhibitory concentration gt 50 mg cntdot L-1) were studied in substrate hydrolysis profile, susceptibility to beta-lactamase inhibitors and isoelectric point (pI) by using ultraviolet spectrophotometry and super-thin layer isoelectric focusing electrophoresis. The results showed that the beta-lactamases from RAzt 1029 and 855 hydrolyzed cephalosporins more strongly than penicillins, could be inhibited by cloxacillin (MCIPC) or Azt, but not by CP45899, pI gt 8.0. It suggested that the enzyme probably belonged to chromosome-mediated Richmond and Sykes type I beta-lactamase (e.g. P99). The beta-lactamase from RAzt 430 hydrolyzed penicillins and cephalosporins equally, could be inhibited by either MCIPC or CP45899. but not by Azt, pI is the same as TEM-1 (5.5). it suggested that the enzyme probably belonged to plasmid -mediated Richmond and Sykes type III beta-lactamase (e.g. TEM-I). The beta-lactamase from RAzt 875 hydrolyzed cephalosporins and penicillins equally, could only be inhibited by the combination (instead of their any single use) of CP45899 and MCIPC or CP45899 and Azt, which presented two bands (pI 8.6 and 5.5) on the isoelectric focusing electrophoresis pattern. It suggested that RAzt 875 had two types of beta-lactamases.

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