The choice of a common endpoint for the recognition of CbE or ChE enzyme activity was made to simplify both reagent preparation and recognition, the only difference between the methods being the nature of the substrate analogue. The ChE activities obtained using the BuTChI for quail blood plasma (Figure 1) are lower than those found by Dieter and Ludke .
The substrate preference of the plasma preparation was measured by comparing rates of reaction with concentrations in the range 0.125, 0.25, 0.5, 1, and 2mM of the substrate analogues AcTChI and BuTChI while in the range 0.25 was 0.5,1,2, and 4 mM for PrTChI and PSA, each of those maybe favourably hydrolysed by different classes of esterase enzyme (Figures 3(a)-3(d)).
Processes for the synthesis of two substrate analogues
including isosteres at the sites of the critical amino acid residues were developed and the substrate analogues
, OMR99-1 and OM99-2, were synthesized.