New Acylate and Thioacylate Effectors of Mammalian Cholinesterases Based on Cyclic Ammonium Alcohols Containing Elements of the Anabasine Structure


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We report a pioneering analysis of the interaction between mammalian cholinesterases and 36 acylates and thioacylates of ammonium alcohols with different structure of an alkyl chain between ammonium and etheric atoms and with different structure of a cyclic ammonium group. Among these ethers, which were both substrates and reversible inhibitors of erythrocyte cholinesterase and serum butyrylcholinesterase, specific effectors of both enzymes were identified.

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N. Basova

Sechenov Institute of Evolutionary Physiology and Biochemistry

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Email: basovn@rambler.ru
俄罗斯联邦, St. Petersburg

B. Kormilitsyn

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
俄罗斯联邦, St. Petersburg

A. Perchenok

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
俄罗斯联邦, St. Petersburg

E. Rozengart

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
俄罗斯联邦, St. Petersburg

V. Saakov

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
俄罗斯联邦, St. Petersburg

A. Suvorov

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: basovn@rambler.ru
俄罗斯联邦, St. Petersburg

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