[Characterization by zymograms of R factor-determined beta-lactamases: plasmids of defined and undefined compatibility groups (author's transl)].
An easy biochemical method is described, discriminating the beta-lacta-mases coded by various R factors. Electrophoretic mobility and substrate affinity of beta-lactamases were studied simultaneously for 7 different penicillins and cephalosporins. They are I like R factors assigned into different compatibility groups (N, P, com6, com7, com8, X and com 9), five R factors isolated from piglets faeces and one R factor, RU1, originated from Enterobacter aerogenes. Three electrophoretic types of beta-lactamases were determinated: 1) beta-lactamase which migrates towards the anode (enzyme coded by Bacillus cereus chromosome); 2) beta-lactamase of weak cathodic mobility (e. g. R6K); 3) beta-lactamase which migrates rapidly towards the cathode (e. g. R46, R71). Escherichia coli K12 strains synthesize a penicillinase of this third type, destroying penicillin G. The enzymatic and physicochemical properties are not modified by host bacteria, suggesting the possibility to study the plasmid in wild bacteria.
D000581:Amidohydrolases / Q000032:analysis*; D002510:Cephalosporinase / Q000032:analysis*; D004352:Drug Resistance, Microbial; D004755:Enterobacteriaceae / Q000201:enzymology*; D004926:Escherichia coli; D007527:Isoenzymes / Q000032:analysis; D010405:Penicillinase / Q000032:analysis*; D011815:R Factors; D012486:Salmonella typhimurium
D007527:Isoenzymes; D000581:Amidohydrolases; D002510:Cephalosporinase; D010405:Penicillinase
Caractérisation par zymogrammes des beta-lactamases déterminées par des facteurs R sauvages ou de référence