Kuleshov VI

References (2)

Title : [Miniature currents of the endplates of the muscle fibers of the diaphragm of the rat after inhibition of acetylcholinesterase with galanthamine] - Krivoi_1985_Neirofiziologiia_17_607
Author(s) : Krivoi II , Kuleshov VI , Matiushkin DP , Sanotskii VI , Sei TP
Ref : Neirofiziologiia , 17 :607 , 1985
Abstract : Miniature end-plate currents (MEPC) in rat diaphragm were studied with voltage-clamp technique when synaptic acetylcholinesterase (AChE) was inhibited with different concentrations of galanthamine. The MEPC amplitude and time course were increased progressively with galanthamine concentrations in the range of 3.16 X 10(-8) - 10(-6) g/ml. The decay of MEPC was always exponential. The input resistance of muscle fibres increased. Galanthamine (10(-5) g/ml) produced a curare-like action: the amplitude and duration of MEPC were less as compared with those at galanthamine concentration 10(-6) g/ml, the decay of MEPC became biphasic. During washing out of the drug, the duration of MEPC began to increase and then to diminish, returning to the initial value 3 hours later. The decay of MEPC became exponential. A positive correlation was found between half-decay time and amplitude of MEPC both in the presence and in the absence of anticholinesterase. It is supposed that the functional role of synaptic AChE in limiting the postsynaptic effect of acetylcholine is not so significant as it is usually considered, therefore it is possible to use the parameters of MEPC for the estimation of functional AChE activity.
ESTHER : Krivoi_1985_Neirofiziologiia_17_607
PubMedSearch : Krivoi_1985_Neirofiziologiia_17_607
PubMedID: 2999623

Title : [Anticholinesterase properties of benzo(f)quinolinium derivatives] - Kuleshov_1981_Biokhimiia_46_1764
Author(s) : Kuleshov VI , Kozlov NS , Libman NM , Kosmacheva IM , Zhikhareva OD
Ref : Biokhimiia , 46 :1764 , 1981
Abstract : In vitro studies have demonstrated that methyl-p-toluene sulfonates of 1-methyl-(ethyl)-3-aryl-benzo(f)quinolinium are highly efficient inhibitors of cholinesterases, the inhibition constants (Ki) for acetylcholinesterase and butyrylcholinesterase being equal to 2.20 +/- 0.49 and 9.43 +/- 0.39 mkM, respectively. The effect of these inhibitors on the enzyme is of competitive - non-competitive type. A certain role in benzo(f)quinoline binding to acetylcholinesterase apparently belongs to the interaction of substituents in the phenyl nucleus with the anionic sites located outside the active surface of the enzyme.
ESTHER : Kuleshov_1981_Biokhimiia_46_1764
PubMedSearch : Kuleshov_1981_Biokhimiia_46_1764
PubMedID: 7306595