Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.8 (cholinesterase)
 12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Organic ammonium salts of N-(2-benzoyloxyethyl)-alkyldimethylammonium bromide (BCHn-1) type are formed by the homological series Ar-COO(CH2)2-N+(CH3)2CnH2a + 1.Br-, whose structure contains a biodegradably labile ester bond, on the basis of which they rank among disinfectants and antiseptics of soft character. They are preferentially biotransformed hydrolytically to produce benzoic acid and substituted choline. The rapidity of enzymatic hydrolysis depends on the chemical structure (the length of the aliphatic chain on the ammonium nitrogen), it increases up to the number of 10 nitrogens of the aliphatic chain, and it rapidly decreases with further prolongation. The paper aimed to demonstrate the catalytic activity of butyrylcholinesterase on the enzymatic hydrolysis of selected organic ammonium salts in the medium of the microsomal fraction of the rat liver on the basis of inhibitory kinetic studies with physostigmine, a cholinesterase inhibitor. The product of enzymatic hydrolysis of BCHn-1, benzoic acid, was determined after extraction with chloroform from the acid medium by means of HPLC analysis with the use of the internal standard p-iodobenzoic acid at the wavelength of 228 nm. Kinetic parameters K(M) and VMAX were evaluated following Lineweaver-Burke using the method of linear regression analysis. The specific activity of butyrylcholinesterase (E.C.3.1.1.8) in the enzymatic hydrolytic process of BCHn-1 was significantly influenced by the presence of physostigmine, which was manifested by increased K(M), KI, and IC50 values in the investigated enzymatic process of selected substrates of the homological series BCHn-1, and by decreased VMAX and rate constants.
 ...
PMID:[Catalytic activity of butyrylcholinesterase in biodegradation of organic ammonium salts in vitro]. 1509 77

A biotinylated organophosphate could be useful for identifying proteins that react with organophosphorus toxicants (OP). FP-biotin, 10-(fluoroethoxyphosphinyl)-N-(biotinamidopentyl)decanamide, was synthesized and found to be stable in methanol and chloroform but less stable in water. Because acetylcholinesterase (AChE, EC 3.1.1.7) and butyrylcholinesterase (BChE, EC 3.1.1.8) are known to be sensitive targets of OP, their reactivity with FP-biotin was tested. The rate constant for reaction with human AChE was 1.8 x 10(7) M(-1) min(-1), and for human BChE, it was 1.6 x 10(8) M(-1) min(-1). A phosphorus stereoisomer, constituting about 50% of the FP-biotin preparation, appeared to be the reactive species. The binding affinity was estimated to be >85 nM for AChE and >5.8 nM for BChE. It was concluded that FP-biotin is a potent OP, well-suited for searching for new biomarkers of OP exposure.
 ...
PMID:Reaction kinetics of biotinylated organophosphorus toxicant, FP-biotin, with human acetylcholinesterase and human butyrylcholinesterase. 1583 35

Haloxylines A (1) and B (2), new piperidine alkaloids, have been isolated from the chloroform soluble fraction of Haloxylon salicornicum and their structures elucidated by spectroscopic techniques including 2D-NMR. Both the compounds displayed antifungal and cholinesterase enzymes inhibitory potentials.
 ...
PMID:Haloxylines A and B, antifungal and cholinesterase inhibiting piperidine alkaloids from Haloxylon salicornicum. 1586 32

Haloxysterols A-D (1-4), new C-24 alkylated sterols, have been isolated from the chloroform soluble fraction of Haloxylon recurvum, along with five known sterols 5-9, which are reported for the first time from this species. Their structures were determined by means of 1D- and 2D-NMR techniques. Compounds 1-9 inhibited cholinesterase enzymes in a concentration-dependent manner with K(i) values ranging between 0.85-25.5 and 1.0-19.0 microM against acetylcholinesterase (AChE; EC 3.1.1.7) and butyrylcholinesterase (BChE; EC 3.1.1.8) enzymes, respectively. Lineweaver-Burk, Dixon plots and their secondary replots indicated that compounds 1-9 are non-competitive inhibitors of both AChE and BChE enzymes.
 ...
PMID:Isolation and cholinesterase-inhibition studies of sterols from Haloxylon recurvum. 1627 89

Slavins A (1) and B (2), the new amyrin type triterpenes, have been isolated from the chloroform soluble fraction of Salvia santolinifolia and assigned structures on the basis of spectral studies including 2D NMR. Both the compounds displayed inhibitory potential against the enzyme butyrylcholinesterase.
 ...
PMID:New butyrylcholinesterase inhibitory triterpenes from Salvia santolinifolia. 1659 90

Prunus persica L. Batsch water extract (PPE) is a potent acetylcholinesterase (AChE) inhibitor screened for the treatment of Alzheimer's disease. The effects of oral administration of the PPE were examined with comparison of those of selective butyrylcholinesterase inhibitors of 9-amino-1,2,3,4-tetrahydroacridine hydrochloride (tacrine) and tetraidopropylpyrophosphoramide (iso-OMPA) and a selective AChE inhibitor, donepezil, on the cholinesterase activity in the brain and plasma of rats. After the sequential solvent fractionation of the methanol extract of P. persica L. Batsch, the highest inhibitory fraction was that of chloroform (75%). The concentration that was required for 50% enzyme inhibition (IC(50) value) was 5.6 microg/mL for the chloroform fraction. Oral administration of PPE or tacrine caused a dose-dependent inhibition of brain and plasma cholinesterase activities. The ID(50) values of these compounds for brain cholinesterase activity were 2.7 g/kg and 8.9 mg/kg, respectively. On the other hand, the ID(50) values for plasma cholinesterase activity were 18.6 g/kg and 27.5 mg/kg, respectively. Thus, the ratios of the ID(50) (plasma < brain) were 6.0 and 3.1, respectively. These results suggest that orally administered PPE satisfactorily penetrates into the brain and inhibits cholinesterase there and that PPE is a potent inhibitor of brain cholinesterase in comparison with plasma cholinesterase in vivo.
 ...
PMID:Pharmacological characterization of orally active cholinesterase inhibitory activity of Prunus persica L. Batsch in rats. 1695 99

In vitro enzymes inhibition activities of the crude methanolic extract and various fractions of Colchicum luteum Baker (Liliaceae) including chloroform, ethyl acetate, n-butanol and aqueous were carried out against actylcholinesterase, butyrylcholinesterase, lipoxygenase and urease enzymes. A significant enzyme inhibition activity (89%) is shown by the crude methanolic extract and its fractions against lipoxygenase, while low to significant activity (32-75%) was evident against butyrylcholinesterase. The crude methanolic extract and its various fractions demonstrated low activity (29-61%) against acetylcholinesterase and no activity against urease.
 ...
PMID:Inhibition activities of Colchicum luteum baker on lipoxygenase and other enzymes. 1705 79

The crude methanolic extract and various fractions of Andrachne cardifolia Muell, including chloroform, ethyl acetate and n-butanol fractions were subjected to in vitro enzyme inhibition activity against acetylcholinesterase, butyrylcholinesterase, lipoxygenase and urease enzymes. A significant enzyme inhibition activity (40-89%) was shown by the crude methanolic extract and its fractions against lipoxygenase, while low to significant activity (40-71%) against butyrylcholinesterase. The crude methanolic extract and its various fractions demonstrated poor to significant activity (25-73%) against acetylcholinesterase and no activity against urease.
 ...
PMID:Enzyme inhibition activities of Andrachne cardifolia Muell. 1751 51

An alcoholic extract obtained from the rhizomes of Gloriosa superba Linn (Colchicaceae) was screened for enzyme inhibition activities. The crude extract and its subsequent fractions including chloroform, ethyl acetate, n-butanol and aqueous were screened against lipoxygenase, actylcholinesterase, butyrylcholinesterase and urease. An outstanding inhibition on lipoxygenase was observed. The highest enzyme inhibition potency was expressed by the chloroform fraction (90%) among the tested fractions on lipoxygenase. Overall 67-90% inhibition was found for lipoxygenase, 46-69% for acetylcholinesterase and 10-33% for butyrylcholinesterase, while urease was not inhibited.
 ...
PMID:Enzyme inhibition activities of the extracts from rhizomes of Gloriosa superba Linn (Colchicaceae). 1823 25

The crude methanolic extract and chloroform, ethyl acetate and n-butanol fractions of Teucrium royleanum were examined as inhibitors of actylcholinesterase, butyrylcholinesterase, lipoxygenase and urease. A significant enzyme inhibition activity (52-83%) was shown by the crude methanolic extract and its fractions against acetylcholinesterase, while low to outstanding enzyme inhibitory activity was shown (19-93%) against butyrylcholinesterase. The crude methanolic extract and its various fractions demonstrated low activity against lipoxygenase and inactive against urease.
 ...
PMID:Enzyme inhibition activities of Teucrium royleanum. 1823 27


<< Previous 1 2 3 4 5 6 Next >>