The acetylcholinesterase (AChE) inhibitor of Yarrowia lipolytica S-3 was maximally produced when it was incubated at 30℃ for 36 h in an optimal medium containing 1% yeast extract, 2% peptone and 2% glucose, with an initial pH 6.0. The final AChE inhibitory activity under these conditions was an IC50 value of 64 mg/ml. After partial purification of the AChE inhibitor by means of systematic solve...

AIM The paper presents research on the most common causes of exposure that leads to disorders of cholinesterase activity, as well as an overview of the results of cholinesterase activity with the poisoned people. MATERIAL AND METHODS In a group of 35 acute poisoned patients by organophosphate compounds has led to inhibition of AchE. A total number of examined workers are 175 in the chemical i...

In this work, the ability of four newly synthesized oximes--K005 (1,3-bis(2-hydroxyiminomethylpyridinium) propane dibromide), K027 (1-(4-hydroxyiminomethylpyridinium)-3-(4-carbamoylpyridinium) propane dibromide), K033 (1,4-bis(2-hydroxyiminomethylpyridinium) butane dibromide) and K048 (1-(4-hydroxyiminomethylpyridinium)-4-(4-carbamoylpyridinium) butane dibromide) to reactivate acetylcholinester...

Background and Objective: Changes of the enzyme acetylcholinesterase are involved in pathogenesis of different nervous disorders including Alzheimer’s disease. This research work was conducted to evaluate the inhibitory effect of Pistacia lentiscus ethanolic extract on acetylcholinesterase activity. Materials and Methods: Activity of the enzyme acetylcholinesterase (AChE) was measured by Ellman...

Administration of oxime therapy is currently the standard approach used to reverse the acute toxicity of organophosphorus (OP) compounds, which is usually attributed to OP inhibition of acetylcholinesterase (AChE). Rate constants for reactivation of OP-inhibited AChE by even the best oximes, such as HI-6 and obidoxime, can vary >100-fold between OP-AChE conjugates that are easily reactivated an...

The cellular structure and distribution of histochemically demonstrated acetylcholinesterase (AChE) activity were studied in the amygdaloid body of 9 dogs. Cytoarchitectonic observations were made in series of paraffin and celloidin sections stained with cresyl violet. For the demonstration of the acetylcholinesterase activity, modifications of Koelle method were used. The general pattern of mo...

Acetylcholinesterase (AChE) exerts noncatalytic activities on neural cell differentiation, adhesion, and neuritogenesis independently of its catalytic function. The noncatalytic functions of AChE have been attributed to its peripheral anionic site (PAS)-mediated protein-protein interactions. Structurally, AChE is highly homologous to the extracellular domain of neuroligin, a postsynaptic transm...

BACKGROUND Peripheral anionic site (PAS) blockade of acetylcholinesterase (AChE) notably affects neuronal activity and cyto-architecture, however, the mechanism(s) involved are incompletely understood. OBJECTIVE We wished to specify the PAS extracellular effects on specific AChE mRNA splice variants, delineate the consequent cellular remodeling events, and explore the inhibitory effects on in...

The expression of acetylcholinesterase (AChE) in skeletal muscle is regulated by muscle activity; however, the underlying molecular mechanisms are incompletely understood. We show here that the expression of the synaptic collagen-tailed AChE form (ColQ-AChE) in quail muscle cultures can be regulated by muscle activity post-translationally. Inhibition of thiol oxidoreductase activity decreases e...

PURPOSE A virtual screening study has suggested that the skeletal muscle relaxant, dantrolene, and the antiemetic drug, ondansetron, may act as inhibitors of the enzyme acetylcholinesterase (AChE). Based on this proposal, the current study examines the AChE inhibitory properties of these drugs. METHODS AND FINDINGS Using AChE from human erythrocytes as enzyme source, it is shown that dantrole...