Inhibition of Acetylcholinesterase by 4,4' -Bipyridine and its Effect upon Phosphylation of the Enzyme
نویسنده
چکیده
The reversible inhibition of acetylcholinesterase (AChE) by 4,4'-bipyridine (BP) was measured with acetylthiocholine as substrate. The enzyme/inhibitor dissociation constant for binding of BP to the catalytic site was Ka = 1.0 mM and the non-competitive dissociation constant for binding to an allosteric site was K, = = 9.0 mM. BP protected AChE against phosphylation by sarin, soman, tabun and VX. The protective effect was also calculated theoretically from a model which assumed that BP reacts either with the catalytic site of the enzyme or with an allosteric site, but does not form a ternary complex with acetylcholinesterase. The calculated and experimentally determined protective indices agreed well.
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