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Lupinine and epilupinine derivatives as substrates of Mammalian cholinesterases

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Pharmaceutical Chemistry Journal Aims and scope

Two series of lupinine and epilupinine acetates, the free bases and the N-methyl, N-ethyl, and N-propyl derivatives, were studied. Enzymatic hydrolysis of substrates by human erythrocyte acetylcholinesterase and horse blood serum butyrylcholinesterase was investigated in comparison with the corresponding dimethylalkyl derivatives of acetylcholine. The important role of non-productive substrate binding was taken into account in the data analysis. Additional information for a better understanding of the metabolism of lupinine derivatives in vivo in animals was obtained.

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Authors and Affiliations

  1. Sechenov Institute of Evolutionary Physiology and Biochemistry, St. Petersburg, Russia

    N. E. Basova, B. N. Kormilitsyn, A. Yu. Perchenok, E. V. Rozengart, V. S. Saakov & A. A. Suvorov

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  1. N. E. Basova
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  2. B. N. Kormilitsyn
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  3. A. Yu. Perchenok
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  4. E. V. Rozengart
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  5. V. S. Saakov
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  6. A. A. Suvorov
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Translated from Khimiko-Farmatsevticheskii Zhurnal, Vol. 46, No. 9, pp. 26 – 28, September, 2012.

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Basova, N.E., Kormilitsyn, B.N., Perchenok, A.Y. et al. Lupinine and epilupinine derivatives as substrates of Mammalian cholinesterases. Pharm Chem J 46, 546–548 (2012). https://doi.org/10.1007/s11094-012-0843-8

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  • DOI: https://doi.org/10.1007/s11094-012-0843-8

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