[Effect of biologically active substances on Escherichia coli chloramphenicol acetyltransferase activity].
The chloramphenicol acetyltransferase activity is mainly localized in the membrane fraction of E. coli 103. Protamine hydrochloride, chlorhexidine, a cationic detergent, and to a less extent nitrofurans lowered the level of the antibiotic inactivation by this strain. Protamine hydrochloride decreased the enzyme activity in both the cell culture of E. coli 103 and the suspension of the membranes isolated from the cells, while chlorhexidine suppressed only induced biosynthesis of chloramphenicol acetyltransferase.
D000123:Acetyltransferases / Q000037:antagonists & inhibitors*; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002701:Chloramphenicol / Q000037:antagonists & inhibitors*; D003600:Cytosol / Q000187:drug effects / Q000201:enzymology; D004352:Drug Resistance, Microbial; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology
D002701:Chloramphenicol; D000123:Acetyltransferases
Vliianie biologicheski aktivnykh veshchestv na aktivnost' khloramfenikol-atsetiltransferazy kishechnoĭ palochki.