Table 3. Inhibition Mechanisms Determined on EeAChE and eqBChE, Inhibition Constants (Ki), and α Values.
EeAChE |
eqBChE |
|||||||||
---|---|---|---|---|---|---|---|---|---|---|
cmpd | mechanism | Ki ± SDa (μM) | R2 | α | cmpd | mechanism | Ki ± SDa (μM) | R2 | α | |
9 | mixed | 0.312 ± 0.108 | 0.982 | 7.5 | 18 | mixed | 3.034 ± 0.604 | 0.986 | 7.3 | |
13 | mixed | 0.426 ± 0.132 | 0.991 | 0.3 | 22 | mixed | 0.099 ± 0.071 | 0.990 | 10 | |
19 | uncomp. | 0.509 ± 0.018 | 0.992 | 25 | mixed | 2.373 ± 0.304 | 0.992 | 2.2 | ||
23 | mixed | 0.743 ± 0.316 | 0.983 | 2.2 | 26 | mixed | 3.465 ± 1.480 | 0.950 | 0.5 | |
25 | mixed | 0.995 ± 0.374 | 0.988 | 0.8 | 28 | mixed | 3.434 ± 0.701 | 0.988 | 0.8 | |
28 | mixed | 1.323 ± 0.622 | 0.990 | 1.2 | 30 | mixed | 1.105 ± 0.189 | 0.983 | 1.4 |
Each data was obtained with three substrate and five inhibitor concentrations; each measurement was carried out in five replicates (see the Experimental Section).