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Inhibition of Acetylcholinesterase by 4,4' -Bipyridine and its Effect upon Phosphylation of the Enzyme

Elsa Reiner ; Institute for Medical Research and Occupational Health, Moše Pijade 158, Zagreb, Croatia, Yugoslavia

Sažetak

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.

Ključne riječi

Hrčak ID:

177278

URI

https://hrcak.srce.hr/177278

Datum izdavanja:

5.11.1986.

Posjeta: 819 *