Abstract
The Inhibition of Hydrolytic Enzymes by Organophosphorus Compounds
Highlights
It hasbeenshownthat severalhydrolytic enzymeswith differ- (b) Trypsin, obtained from Worthington Biochemical Corent specificitiesundergosimilarreactionswith diisopropyl phos- poration as a twice crystallized material, was assayedas for phorofluoridate [1] and other related toxic organophosphorus chymotrypsin [7]
Are presented in Fig. 1 where the logarithmic scale of inhibitor concentration shows the wide differences in the rates of reaction of the inhibitor with the various enzymes
More information can be obtained from this figure when it is considered in relation to the experimental conditions
Summary
Inhibitor substrate; other sampleswere precipitated at intervals during (0.1 ml) and enzyme (0.2 ml) were incubated together for 30 a periodof 1 hour. The enzyme concentration was 25 mg per ml and 0.2 ml of this solution was incubated in the side arm of the flask with 0.1 ml of inhibitor for 30 minutes at 37” before tipping. If the concentration of enzyme, pH, and time of reaction are kept constant, the extent of inhibition in a particular system is proportional to the concentration of inhibitor [2]. Mounter observed in each determination was plotted against the negative logarithm of the inhibitor concentration The intercepts of these curves with the lines representing 50 y0 and 30 y0 inhibition gave the values of ~150 and pIso, respectively (Fig. 1). The 1)1x0 value indicates the extent of inhibition for slow reactions where high degrees of inactivation may not be observed due to limitations of inhibitor concentration or time of reaction
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