Zobrazeno 1 - 10
of 16
pro vyhledávání: '"A. Yu. Perchenok"'
Autor:
N. E. Basova, B. N. Kormilitsyn, A. Yu. Perchenok,, E. V. Rozengart, V. S. Saakov, A. A. Suvorov
Publikováno v:
The Ukrainian Biochemical Journal, Vol 86, Iss 5, Pp 47-55 (2014)
Specifically synthesized group of benzimidazole derivatives possessing varying degrees of delocalization of the positive charge in the cation group of the molecule has been studied in order to search for potential cholinergically active compounds a
Externí odkaz:
https://doaj.org/article/fb03b2ede9534071ba807b2e68b8f2ae
Autor:
B. N. Kormilitsyn, Vladimir S. Saakov, E. V. Rozengart, N. E. Basova, A. A. Suvorov, A. Yu. Perchenok
Publikováno v:
Journal of Evolutionary Biochemistry and Physiology. 54:157-174
This review summarizes the literature data as well as experimental results obtained at our Institute over a period of 50 years on the substrate specificity of cholinesterases–acetylcholine acetylhydrolases (EC 3.1.1.7) and acylcholine acylhydrolase
Autor:
A. A. Suvorov, A. Yu. Perchenok, N. E. Basova, Vladimir S. Saakov, B. N. Kormilitsyn, E. V. Rozengart
Publikováno v:
Journal of Evolutionary Biochemistry and Physiology. 54:22-29
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
Autor:
E. V. Rozengart, A. Yu. Perchenok, A. A. Suvorov, B. N. Kormilitsyn, Vladimir S. Saakov, N. E. Basova
Publikováno v:
Pharmaceutical Chemistry Journal. 50:509-512
Inorganic tetramethylene bis-onium compounds were studied as reversible inhibitors of various cholinesterases (ChE), i.e., human erythrocyte acetyl-ChE, horse blood serum butyryl-ChE, grass frog Rana temporaria brain ChE, and Pacific squid Todarodes
Autor:
A. Yu. Perchenok, A. A. Suvorov, N. E. Basova, B. N. Kormilitsyn, E. V. Rozengart, Vladimir S. Saakov
Publikováno v:
Journal of Evolutionary Biochemistry and Physiology. 52:346-351
To study the effect of the onium atom nature on anticholinesterase efficiency, we tested elementorganic derivatives of tetramethylenbisonium compounds as reversible inhibitors of the following cholinesterases (ChE): acetyl-ChE from human erythrocytes
Publikováno v:
Zhurnal evoliutsionnoi biokhimii i fiziologii. 52(5)
To study the influence of onium atom nature on anticholinesterase efficiency of elementorganic derivatives of tetramethylenbisonium compounds as reversible inhibitors of cholinesterase (ChE) - acetyl-ChE from human erythrocytes, butyryl-ChE from hors
Autor:
Rozengart Ev, A. Yu. Perchenok, N. E. Basova, B. N. Kormilitsyn, A. A. Suvorov, Vladimir S. Saakov
Publikováno v:
Scopus-Elsevier
The review presents data on comparative reactivity of 68 cholinesterase preparation from various organs and tissues in a number of vertebrates and invertebrates based on sensitivity to two highly specific and most studied organophosphorus inhibitors-
Autor:
B. N. Kormilitsyn, N. E. Basova, E. V. Rozengart, Vladimir S. Saakov, A. A. Suvorov, A. Yu. Perchenok
Publikováno v:
Journal of Evolutionary Biochemistry and Physiology. 50:20-26
The study was performed to check whether the horse blood serum butyrylcholinesterase expresses transferase activity in the presence of several low-molecular aliphatic alcohols, using chromogenic substrate 1-methyl-8-acetoxychinolium iodide whose phen
Autor:
N. E. Basova, B. N. Kormilitsyn, A. A. Suvorov, A. Yu. Perchenok, Vladimir S. Saakov, E. V. Rozengart
Publikováno v:
Journal of Evolutionary Biochemistry and Physiology. 49:481-488
There was studied action of aliphatic alcohols (ethanol, propanol, isopropanol, n-butanol, isobutanol, sec-butanol, tert-butanol), and pH on various kinds of serum cholinesterase. At inhibition of the cholinesterase hydrolytic activity under effect o
Publikováno v:
Zhurnal evoliutsionnoi biokhimii i fiziologii. 51(6)
The review presents data on comparative reactivity of 68 cholinesterase preparation from various organs and tissues in a number of vertebrates and invertebrates based on sensitivity to two highly specific and most studied organophosphorus inhibitors-