. Author manuscript; available in PMC: 2016 Mar 1.

Published in final edited form as: Biochem J. 2013 Feb 15;450(1):231–242. doi: 10.1042/BJ20121612

Table 1.

Kinetic constants for reactivation of paraoxon-, sarin-, cyclosarin-,VX- and tabun-hBChE and hAChE conjugates by non-pyridinium oxime TAB2OH and reference oxime 2PAM; inhibition constants, K_i and αK_i, (mM),of native AChE and BChE (without OP) by two oximes. Maximal reactivation rate constant (k₂, min⁻¹), apparent dissociation constant of [oxime * OP-hAChE conjugate] reversible complex (K_ox, mM) and overall second order reactivation rate constant (k_r, M⁻¹min⁻¹) were determined from reactivation curves as presented in Figure 3 and Figure S1. All constants were determined from triplicate experiments in 0.1M phosphate pH 7.4, 37°C. Standard errors of determined kinetic constants were typically less than 30% of the mean.

Oxime	enzyme	Paraoxon			Sarin			Cyclosarin			VX			Tabun			without OP
Oxime	enzyme	k₂	K_ox	k_r	k₂	K_ox	k_r	k₂	K_ox	k_r	k₂	K_ox	k_r	k₂	K_ox	k_r	K_i	αK_i
TAB2OH	BChE	0.34	0.71	480	0.19	0.79	250	3.9	1.0	3700	2.0	1.5	1300	0.00027	1.3	0.21	0.32	0.74
2PAM	BChE	0.23	2.4	96	2.4	1.8	1300	2.6	5.4	480	1.2	2.5	480	0.0011	1.2	0.91	0.23	18
TAB2OH	AChE	0.47	12	41	0.92	27	34	0.44	36	12	2.4	23	100	0.0032	8.2	0.39	0.20	4.0
2PAM	AChE	0.27	1.8	150	1.1	0.34	3300	0.73	6.6	110	0.74	0.32	2300	0.0058	1.6	3.8	0.34	1.9