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Specificity of the interaction of ephedrine based and pseudoephedrine based choline analogs and acetylcholinesterase and butyrylcholinesterase






Doklady Akademii Nauk SSSR 289(1): 227-230

Specificity of the interaction of ephedrine based and pseudoephedrine based choline analogs and acetylcholinesterase and butyrylcholinesterase

The effect of the conformational properties and the optical activity of ephedrine- and pseudoephedrine-based choline analogs on the reversible inhibitory activity with respect to acetylcholinesterase and butyrylcholinesterase was studied. Acetylcholinesterase from human blood erythrocytes and butylcholinesterase from the equine blood serum were used in the experiment. All the compounds under study were competitive reversible inhibitors of both enzymes. Anticholinesterase activity significantly depends on the environment of the N atom. A reduction of the rotation angle value causes a significant decrease in anticholinesterase activity of the erythro-form and threo-form of ephedrine derivatives. Erythro-derivatives of ephedrine were more active with respect to acetylcholinesterase than threo-derivatives. The anionic site of the active center of butylrylcholinesterase was less specific with respect to stereoisomers.


Accession: 006459092



Related references

Dalimov, D.N.; Vaĭzburg, G.M.; Abdullaeva, L.K.; Abduvakhabov, A.A.; Sadykov, A.S., 1986: Specificity of interaction with acetylcholinesterase and butyrylcholinesterase of choline analogs based on ephedrine and pseudoephedrine. Doklady Akademii Nauk SSSR 289(1): 227-230

Harel, M.; Silman, I.; Sussman, J.L., 1992: A model of butyrylcholinesterase based on the X-ray structure of acetylcholinesterase indicates differences in specificity. Shafferman, A [Editor], Velan, B [Editor] Multidisciplinary approaches to cholinesterase functions : 189-194

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