Etude électrophorétique de la butyrylcholinestérase agée après inhibition par le soman

Butyrylcholinesterase for protection from organophosphorus poisons: Catalytic complexities and hysteretic behavior

“…Procainamide was selected as a ligand for affinity column purification because the inhibition constant for procainamide (Ki = 9×10 −6 M) [25,26] is tight enough to give good binding, but not so tight as to make it impossible to release the bound butyrylcholinesterase. The procainamide affinity column does not purify butyrylcholinesterase in a single step.…”

“…Cross-linking of butyrylcholinesterase with dimethylimidates of different chain length showed that upon aging there was no change in the quaternary structure of butyrylcholinesterase or in the overall conformation of subunits [26]. However, enzyme denaturation studies showed that the conformational stability of aged cholinesterase is dramatically increased compared to non-inhibited and non-aged enzymes [84–87].…”

Butyrylcholinesterase for protection from organophosphorus poisons: Catalytic complexities and hysteretic behavior

“…Procainamide was selected as a ligand for affinity column purification because the inhibition constant for procainamide (Ki = 9×10 −6 M) [25,26] is tight enough to give good binding, but not so tight as to make it impossible to release the bound butyrylcholinesterase. The procainamide affinity column does not purify butyrylcholinesterase in a single step.…”

“…Cross-linking of butyrylcholinesterase with dimethylimidates of different chain length showed that upon aging there was no change in the quaternary structure of butyrylcholinesterase or in the overall conformation of subunits [26]. However, enzyme denaturation studies showed that the conformational stability of aged cholinesterase is dramatically increased compared to non-inhibited and non-aged enzymes [84–87].…”

Butyrylcholinesterase for protection from organophosphorus poisons: Catalytic complexities and hysteretic behavior

“…Procainamide was selected as a ligand for affinity column purification because the inhibition constant for procainamide (Ki = 9×10 −6 M) [25,26] is tight enough to give good binding, but not so tight as to make it impossible to release the bound butyrylcholinesterase. The procainamide affinity column does not purify butyrylcholinesterase in a single step.…”

“…Cross-linking of butyrylcholinesterase with dimethylimidates of different chain length showed that upon aging there was no change in the quaternary structure of butyrylcholinesterase or in the overall conformation of subunits [26]. However, enzyme denaturation studies showed that the conformational stability of aged cholinesterase is dramatically increased compared to non-inhibited and non-aged enzymes [84–87].…”

Butyrylcholinesterase for protection from organophosphorus poisons: Catalytic complexities and hysteretic behavior

“…Procainamide was selected as a ligand for affinity column purification because the inhibition constant for procainamide (Ki = 9×10 −6 M) [25,26] is tight enough to give good binding, but not so tight as to make it impossible to release the bound butyrylcholinesterase. The procainamide affinity column does not purify butyrylcholinesterase in a single step.…”

“…Cross-linking of butyrylcholinesterase with dimethylimidates of different chain length showed that upon aging there was no change in the quaternary structure of butyrylcholinesterase or in the overall conformation of subunits [26]. However, enzyme denaturation studies showed that the conformational stability of aged cholinesterase is dramatically increased compared to non-inhibited and non-aged enzymes [84–87].…”