Biomolecular rate constant for reactivation and measure of the inherent reactivity of the oximate form of the reactivator at the concentration 1.00 mM [HOX] in the conditions of 25degreeC,pH 7.6
Kinetic constant(1/ K obsd (min)) was calculated for the observed reaction rate constant at the concentration 0.0500 mM [HOX] in the conditions of 25degreeC,pH 7.6
Kinetic constant(1/ K obsd (min)) was calculated for the observed reaction rate constant at the concentration 0.100 mM [HOX] in the conditions of 25degreeC,pH 7.6
Kinetic constant(1/ K obsd (min)) was calculated for the observed reaction rate constant at the concentration 0.500 mM [HOX] in the conditions of 25degreeC,pH 7.6
Kinetic constant(1/ K obsd (min)) was calculated for the observed reaction rate constant at the concentration 1.00 mM [HOX] in the conditions of 25degreeC,pH 7.6
Kinetic constant(1/ [OX](1/min)) was calculated for the dissociated oximate form at the concentration 0.0500 mM [HOX] in the conditions of 25degreeC,pH 7.6
Kinetic constant(1/ [OX](1/min)) was calculated for the dissociated oximate form at the concentration 0.100 mM [HOX] in the conditions of 25degreeC,pH 7.6
Kinetic constant(1/ [OX](1/min)) was calculated for the dissociated oximate form at the concentration 0.500 mM [HOX] in the conditions of 25degreeC,pH 7.6
Kinetic constant(1/ [OX](1/min)) was calculated for the dissociated oximate form at the concentration 1.00 mM [HOX] in the conditions of 25degreeC,pH 7.6
Concentration at 10 uM that inhibits 50%of acetylcholinesterase activity evaluated in vitro at a pH of 8 in the presence of 7.5x10E-4 acetylthiocholine
Concentration at 25 uM that inhibits 50%of acetylcholinesterase activity evaluated in vitro at a pH of 8 in the presence of 7.5x10E-4 acetylthiocholine