RESUMEN
Solutions of glucose-3-phosphate dehydrogenase (GPD) and pectin methylesterase (PME) were exposed to various anesthetics and dichlorodifluoromethane (F-12) to determine the abilities of these chemicals to inhibit enzyme activity. An aqueous solution of PME was exposed to saturation levels of the test chemicals for 30 min at 21 degrees. All test chemicals were inhibitory (measured after release of the test chemical) with propane being most inhibitory followed in order by F-12, cyclopropane, Ethrane (F2HCOF2CCHClF) and halothane (CF3CHClBr). GPD was exposed to various concentrations of F-12 and halothane for various times at 0 degrees and 33 degrees. Halothane at 33 degrees and a saturation concentration reduced the initial reaction velocity of GPD to zero after a 10-min exposure period. F-12 was somewhat less inhibitory than halothane, but inhibition in all instances was irreversible. Halothane was found to affect the circular dichroism and optical rotary dispersion spectra of GPD, with the magnitude of the changes generally increasing with treatment time. The observed changes were believed to arise from side-chain transitions of GPD.
Asunto(s)
Anestésicos/farmacología , Hidrolasas de Éster Carboxílico/antagonistas & inhibidores , Clorofluorocarburos de Metano/farmacología , Gliceraldehído-3-Fosfato Deshidrogenasas/antagonistas & inhibidores , Dicroismo Circular , Difusión , Halotano/farmacología , Dispersión Óptica Rotatoria , TemperaturaRESUMEN
Three anaesthetics (halothane, CF3CHClBr; Ethrane, F2 HCOF2CCHClF; cyclopropane) and one other halogenated, short-chain hydrocarbon (F-12, Cl2F2C) were tested under various conditions to determine their effects on the viability of cells of Escherichia coli and the activities of some of its enzymes. When any of the test chemicals were applied for 60 min at concentrations slightly in excess of saturation, the number of surviving cells decreased substantially, with halothane being the most biocidal of the four chemicals and F-12 the least. Three enzymes (malate dehydrogenase, MD; NADH dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase, GPD) were tested for activity after treatment of E. coli with the test chemicals. In all instances, GPD was least resistant to inactivation and MD was most resistant. Halothane was most inhibitory followed in order by Ethrane, cyclopropane and F-12. Treatment of E. coli with halothane for 60 min at 23 degrees C and a concentration slightly in excess of saturation, resulted in nearly complete inhibition of all three enzymes.