. Author manuscript; available in PMC: 2012 Nov 1.

Published in final edited form as: Protein Expr Purif. 2011 Jul 23;80(1):22–27. doi: 10.1016/j.pep.2011.07.005

Table 2.

Kinetic parameters of FL and W541H₆Δ BChE enzymes using BTC as a substrate

Enzyme	p value^a	K_M, μM	K_SS, mM	b
Wild-type	0.3	27 ± 5	1.06 ± 0.15	2.6 ± 0.2
W541H₆Δ	0.3	40 ± 6	1.16 ± 0.17	2.3 ± 0.2

G117H	0.5	170 ± 12	1.2 ± 0.2	2.2^b
G117H, W541H₆Δ	0.5	181 ± 8	1.3 ± 0.1	2.2

G117H/E197Q	0.9	710 ± 20	120^c	5^c
G117H/E197Q, W541H₆Δ	0.9	710 ± 10	120^c	5^c

Enzymatic BTC hydrolysis was monitored at room temperature in PBS, pH 7.4, and the observed rates of hydrolysis were fit to Eq. 1. The listed best fit values and fitting errors resulted from a single determination for each enzyme (18 to 24 data points).

The indicated p values resulted from comparison of the kinetic data sets for the indicated pairs of enzymes using the sum-of-squares F test.

The b value was constrained at a value of 2.2.

The indicated parameters were assigned based on the report by Millard et al., 1998 [9].