PL
W pracy przedstawiono wyniki badań dotyczących hamowania dehydrogenazy alkoholowej jako enzymu pierwszego etapu biotransformacji alkoholi. Sprawdzono skuteczność następujących związków: fenylohydrazyny, acetylo-L-karnityny, 1,10-fenantroliny, amidu kwasu izowalerianowego, EDTA, dimetylosulfotlenku i penicylaminy w stężeniach 1,0; 0,10; 0,01 mol/dm3. Substratami enzymu był metanol w stężeniach 0,10 i 0,05 mol/dm3 oraz glikol etylenowy w stężeniu 0,10 mol/dm3.
EN
A rational management of alcohol intoxication could be based on the inhibition of alcohol hydrogenase (ADH), the first enzyme involved in the biotransformation of alcohols. Standard therapy for methanol and ethylene glycol intoxication comprises administration of ethanol to inhibit their oxidation by ADH to more toxic metabolites. The aim of this work was to find some human liver ADH inhibitors, other than ethanol. In the present study, ADH activity was estimated by spectrophotometry by assessing NADH absorbance in vitro at pH 7.4 and 37°C using human enzyme hepatic fraction. The inhibiting effect of six selected chemical compounds on ADH was tested and the residual activity of the enzyme inhibited by the selected chemicals in the reaction with 0.05 mol/dm3 and 0.10 mol/dm3 methanol and 0.10 mol/dm3 ethylene glycol as substrates was determined. The ADH activity was, to a varying extent, inhibited by all examined chemicals: acetyl-L carnitine, o-phenantroline, isovaleric acid amide, DMSO, EDTA, phenylohydrazine and penicillamine at 1.0; 0.10; 0.01 mmol/dm3. O-phenantroline proved to be the best inhibitor, both in the reaction with methanol and ethylene glycol.