Acetylthiocholine
Acetylcholinesterase
Tetraisopropylpyrophosphamide
Cholinesterase Inhibitors
Drugs that inhibit cholinesterases. The neurotransmitter ACETYLCHOLINE is rapidly hydrolyzed, and thereby inactivated, by cholinesterases. When cholinesterases are inhibited, the action of endogenously released acetylcholine at cholinergic synapses is potentiated. Cholinesterase inhibitors are widely used clinically for their potentiation of cholinergic inputs to the gastrointestinal tract and urinary bladder, the eye, and skeletal muscles; they are also used for their effects on the heart and the central nervous system.
Thiocholine
Substrate Specificity
Powders
Electrophorus
Electric Organ
In about 250 species of electric fishes, modified muscle fibers forming disklike multinucleate plates arranged in stacks like batteries in series and embedded in a gelatinous matrix. A large torpedo ray may have half a million plates. Muscles in different parts of the body may be modified, i.e., the trunk and tail in the electric eel, the hyobranchial apparatus in the electric ray, and extrinsic eye muscles in the stargazers. Powerful electric organs emit pulses in brief bursts several times a second. They serve to stun prey and ward off predators. A large torpedo ray can produce of shock of more than 200 volts, capable of stunning a human. (Storer et al., General Zoology, 6th ed, p672)
Receptors, Cholinergic
Cell surface proteins that bind acetylcholine with high affinity and trigger intracellular changes influencing the behavior of cells. Cholinergic receptors are divided into two major classes, muscarinic and nicotinic, based originally on their affinity for nicotine and muscarine. Each group is further subdivided based on pharmacology, location, mode of action, and/or molecular biology.
Research Report
Databases, Protein
Internet
User-Computer Interface
Software
Proteins
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Sydnones
Cyclization
Benzo(a)pyrene
Memory Disorders
PubMed
A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.
Publishing
MEDLINE
Protein Array Analysis
Autoantibodies
Oligonucleotide Array Sequence Analysis
Amphotericin B
Culture Media
Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.
Epithelial Cells
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
Pyruvic Acid
Streptomycin
Hepatitis, Infectious Canine
Glycogen Phosphorylase, Muscle Form
Dog Diseases
Histochemically distinct compartments in the striatum of human, monkeys, and cat demonstrated by acetylthiocholinesterase staining. (1/38)
We here report observations on the distribution of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) in the striatum of the adult human, the rhesus monkey, and the cat. By the histochemical staining methods of Geneser-Jensen and Blackstad and of Karnovsky and Roots, compartments of low cholinesterase activity were identified in parts of the striatum in all three species. In frontal sections, these enzyme-poor zones appeared as a variable number of weakly stained approximately 0.5-mm-wide zones embedded in a darkly stained background. The zones varied in cross-sectional shape from round to elongated and were sometimes branched. They were most prominent in the head of the caudate nucleus. Three-dimensional reconstructions of serial sections through the caudate nucleus in the human and cat suggest that over distances of at least several millimeters, the zones of low enzyme activity form nearly continuous labyrinths. (+info)Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis. (2/38)
We recently reported on a non-neuronal secreted acetylcholinesterase (AChE B) from the nematode parasite Nippostrongylus brasiliensis. Here we describe the primary structure and enzymatic properties of a second secreted variant, termed AChE C after the designation of native AChE isoforms from this parasite. As for the former enzyme, AChE C is truncated at the carboxyl terminus in comparison with the Torpedo AChE, and three of the 14 aromatic residues that line the active site gorge are substituted by nonaromatic residues, corresponding to Tyr70 (Ser), Trp279 (Asn) and Phe288 (Met). A recombinant form of AChE C was highly expressed by Pichia pastoris. The enzyme was monomeric and hydrophilic, and displayed a marked preference for acetylthiocholine as substrate. A double mutation (W302F/W345F, corresponding to positions 290 and 331 in Torpedo) rendered the enzyme 10-fold less sensitive to excess substrate inhibition and two times less susceptible to the bis quaternary inhibitor BW284C51, but did not radically affect substrate specificity or sensitivity to the 'peripheral site' inhibitor propidium iodide. In contrast, a triple mutant (M300G/W302F/W345F) efficiently hydrolysed propionylthiocholine and butyrylthiocholine in addition to acetylthiocholine, while remaining insensitive to the butyrylcholinesterase-specific inhibitor iso-OMPA and displaying a similar profile of excess substrate inhibition as the double mutant. These data highlight a conserved pattern of active site architecture for nematode secreted AChEs characterized to date, and provide an explanation for the substrate specificity that might otherwise appear inconsistent with the primary structure in comparison to other invertebrate AChEs. (+info)High-resolution optical mapping of the right bundle branch in connexin40 knockout mice reveals slow conduction in the specialized conduction system. (3/38)
Connexin40 (Cx40) is a major gap junction protein that is expressed in the His-Purkinje system and thought to be a critical determinant of cell-to-cell communication and conduction of electrical impulses. Video maps of the ventricular epicardium and the proximal segment of the right bundle branch (RBB) were obtained using a high-speed CCD camera while simultaneously recording volume-conducted ECGs. In Cx40(-/-) mice, the PR interval was prolonged (47.4+/-1.4 in wild-type [WT] [n=6] and 57.5+/-2.8 in Cx40(-/-) [n=6]; P<0.01). WT ventricular epicardial activation was characterized by focused breakthroughs that originated first on the right ventricle (RV) and then the left ventricle (LV). In Cx40(-/-) hearts, the RV breakthrough occurred after the LV breakthrough. Additionally, Cx40(-/-) mice showed RV breakthrough times that were significantly delayed with respect to QRS complex onset (3.7+/-0.7 ms in WT [n=6] and 6.5+/-0.7 ms in Cx40(-/-) [n=6]; P<0.01), whereas LV breakthrough times did not change. Conduction velocity measurements from optical mapping of the RBB revealed slow conduction in Cx40(-/-) mice (74.5+/-3 cm/s in WT [n=7] and 43.7+/-6 cm/s in Cx40(-/-) [n=7]; P<0.01). In addition, simultaneous ECG records demonstrated significant delays in Cx40(-/-) RBB activation time with respect to P time (P-RBB time; 41.6+/-1.9 ms in WT [n=7] and 55.1+/-1.3 ms in [n=7]; P<0.01). These data represent the first direct demonstration of conduction defects in the specialized conduction system of Cx40(-/-) mice and provide new insight into the role of gap junctions in cardiac impulse propagation. (+info)Action potential characteristics and arrhythmogenic properties of the cardiac conduction system of the murine heart. (4/38)
Studies have characterized conduction velocity in the right and left bundle branches (RBB, LBB) of normal and genetically engineered mice. However, no information is available on the action potential characteristics of the specialized conduction system (SCS). We have used microelectrode techniques to characterize action potential properties of the murine SCS, as well as epicardial and endocardial muscle preparations for comparison. In the RBB, action potential duration at 50%, 70%, and 90% repolarization (APD(50,70,90)) was 6+/-0.7, 35+/-6, and 90+/-7 ms, respectively. Maximum upstroke velocity (dV/dt(max)) was 153+/-14 V/s, and conduction velocity averaged 0.85+/-0.2 m/s. APD(90) was longer in the Purkinje network of fibers (web) than in the RBB (P<0.01). Web APD(50) was longer in the left than in the right ventricle (P<0.05). Yet, web APD(90) was longer in the right than in the left ventricle (P<0.001). APD(50,70) was significantly longer in the endocardial than in the epicardial (P<0.001; P<0.003). APD(90) in the epicardial and endocardial was shorter than in the RBB ( approximately 36 ms versus approximately 100 ms). Spontaneous electrical oscillations in phase 2 of the SCS occasionally resulted in early afterdepolarizations. These results demonstrate that APDs in the murine SCS are significantly ( approximately 2-fold) longer than in the myocardium and implicate the role of the murine SCS in arrhythmias. The differences should have important implications in the use of the mouse heart to study excitation, propagation, and arrhythmias. (+info)Reversibly bound and covalently attached ligands induce conformational changes in the omega loop, Cys69-Cys96, of mouse acetylcholinesterase. (5/38)
We have used a combination of cysteine substitution mutagenesis and site-specific labeling to characterize the structural dynamics of mouse acetylcholinesterase (mAChE). Six cysteine-substituted sites of mAChE (Leu(76), Glu(81), Glu(84), Tyr(124), Ala(262), and His(287)) were labeled with the environmentally sensitive fluorophore, acrylodan, and the kinetics of substrate hydrolysis and inhibitor association were examined along with spectroscopic characteristics of the acrylodan-conjugated, cysteine-substituted enzymes. Residue 262, being well removed from the active center, appears unaffected by inhibitor binding. Following the binding of ligand, hypsochromic shifts in emission of acrylodan at residues 124 and 287, located near the perimeter of the gorge, reflect the exclusion of solvent and a hydrophobic environment created by the associated ligand. By contrast, the bathochromic shifts upon inhibitor binding seen for acrylodan conjugated to three omega loop (Omega loop) residues 76, 81, and 84 reveal that the acrylodan side chains at these positions are displaced from a hydrophobic environment and become exposed to solvent. The magnitude of fluorescence emission shift is largest at position 84 and smallest at position 76, indicating that a concerted movement of residues on the Omega loop accompanies gorge closure upon ligand binding. Acrylodan modification of substituted cysteine at position 84 reduces ligand binding and steady-state kinetic parameters between 1 and 2 orders of magnitude, but a similar substitution at position 81 only minimally alters the kinetics. Thus, combined kinetic and spectroscopic analyses provide strong evidence that conformational changes of the Omega loop accompany ligand binding. (+info)Asymmetric distribution of acetylcholinesterase in gravistimulated maize seedlings. (6/38)
Acetylcholinesterase (AChE) activity has previously been studied by this laboratory and shown to occur at the interface between the stele and cortex of the mesocotyl of maize (Zea mays L.) seedlings. In this work we studied the distribution of AChE activity in 5-d-old maize seedlings following a gravity stimulus. After the stimulus, we found an asymmetric distribution of the enzyme in the coleoptile, the coleoptile node, and the mesocotyl of the stimulated seedlings using both histochemical and colorimetric methods for measuring the hydrolysis of acetylthiocholine. The hydrolytic capability of the esterase was greater on the lower side of the horizontally placed seedlings. Using the histochemical method, we localized the hydrolytic capability in the cortical cells around the vascular stele of the tissues. The hydrolytic activity was inhibited 80 to 90% by neostigmine, an inhibitor of AChE. When neostigmine was applied to the corn kernel, the gravity response of the seedling was inhibited and no enzyme-positive spots appeared in the gravity-stimulated seedlings. We believe these results indicate a role for AChE in the gravity response of maize seedlings. (+info)Studies of the acetylcholinesterase from houseflies (Musca domestica L.) resistant and susceptible to organophosphorus insecticides. (7/38)
Acetylcholinesterase from the heads of insecticide-resistant and -susceptible houseflies (Musca domestica L.) was studied in vitro. The enzymes could not be distinguished electrophoretically, and their behaviour on polyacrylamide-disc-gel electrophoresis was influenced by the presence of Triton X-100 in both the homogenate and the gels. In the absence of detergent, the acetylcholinesterase was heterogeneous, but behaved as a single enzyme when it was present. By analogy with studies of acetylcholinesterase from other sources, these observations were attributed to aggregation of the enzyme when not bound by membranes. The enzyme from resistant flies was more slowly inhibited than the susceptible enzyme, bimolecular rate constants (ki) differing by approx. 4-20-fold for a range of organophosphorus compounds. The kinetics of inhibition of acetylcholinesterase were consistent with the results of electrophoresis, i.e. they corresponded to those of a single enzyme in the presence of Triton X-100, but a mixture of enzymes in its absence. The susceptibility of the more sensitive components in these mixtures was determined. (+info)Substrate activation in acetylcholinesterase induced by low pH or mutation in the pi-cation subsite. (8/38)
Substrate inhibition is considered a defining property of acetylcholinesterase (AChE), whereas substrate activation is characteristic of butyrylcholinesterase (BuChE). To understand the mechanism of substrate inhibition, the pH dependence of acetylthiocholine hydrolysis by AChE was studied between pH 5 and 8. Wild-type human AChE and its mutants Y337G and Y337W, as well as wild-type Bungarus fasciatus AChE and its mutants Y333G, Y333A and Y333W were studied. The pH profile results were unexpected. Instead of substrate inhibition, wild-type AChE and all mutants showed substrate activation at low pH. At high pH, there was substrate inhibition for wild-type AChE and for the mutant with tryptophan in the pi-cation subsite, but substrate activation for mutants containing small residues, glycine or alanine. This is particularly apparent in the B. fasciatus AChE. Thus a single amino acid substitution in the pi-cation site, from the aromatic tyrosine of B. fasciatus AChE to the alanine of BuChE, caused AChE to behave like BuChE. Excess substrate binds to the peripheral anionic site (PAS) of AChE. The finding that AChE is activated by excess substrate supports the idea that binding of a second substrate molecule to the PAS induces a conformational change that reorganizes the active site. (+info)
Sensors | Free Full-Text | Critical Evaluation of Acetylthiocholine Iodide and Acetylthiocholine Chloride as Substrates for...
Acetylthiocholine chloride ≥99% (TLC), powder | 6050-81-3
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AID 1085535 - Inhibition of Electrophorus electricus (electric eel) acetylcholinesterase (AChE) using acetylthiocholine iodide...
Substrate activation in acetylcholinesterase induced by low pH or mutation in the π-cation subsite<...
中国科学院大连化学物理研究所机构知识库(DICP OpenIR): Fundamental Reaction Pathway and Free Energy Profile for Butyrylcholinesterase-Catalyzed...
Preliminary investigation on cholinesterase activity in Adamussium colbecki from Terra Nova Bay: field and laboratory study |...
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Sensors | Free Full-Text | Variation of Cholinesterase-Based Biosensor Sensitivity to Inhibition by Organophosphate Due To...
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Cerebral acetylcholinesterase activity is not decreased in MS patients with cognitive impairment.
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Acetylcholinesterase (AChE) 425011
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Simple general acid-base catalysis of physiological acetylcholinesterase reactions<...
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Carbofuran-induced effects on acetylcholinesterase (AChE) in erythrocytes and liver of Cyprinus carpio | KSU Faculty
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Acetylcholinesterase in motion : Visualizing conformational changes in crystal structures by a morphing procedure
Structures of the Acyl−Enzyme Complexes of the
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Overlapping drug interaction sites of human butyrylcholinesterase dissected by site-directed mutagenesis. - Semantic Scholar
Acetylcholinesterase Inhibitors with Photoswitchable Inhibition of β‑Amyloid Aggregation - University of Regensburg...
6-Methyluracil derivatives as acetylcholinesterase inhibitors for treatment of Alzheimers disease | Read by QxMD
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Acetylcholinesterase - definition of acetylcholinesterase by The Free Dictionary
RCSB PDB
- 1PWD: Covalent acyl enzyme complex of the Streptomyces R61 DD-peptidase with cephalosporin C Macromolecule...
Structure Cluster
- 1PWC: penicilloyl acyl enzyme complex of the Streptomyces R61 DD-peptidase with penicillin G 3D...
Synthesis and biological evaluation of 8-hydroxy-2,7-naphthyridin-2-ium salts as novel inhibitors of acetylcholinesterase (AChE...
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Mouse (Murine) Acetylcholinesterase (AChE) Protein, Recombinant | ABIN6301593
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Acetylthiocholine
... is an acetylcholine analog used in scientific research. "Acetylthiocholine - MeSH - NCBI". www.ncbi.nlm.nih. ... "Reaction Pathway and Free Energy Profiles for Butyrylcholinesterase-Catalyzed Hydrolysis of Acetylthiocholine". Biochemistry. ...
Acetylthiocholine - Wikipedia
Acetylthiocholine chloride ≥99% (TLC), powder | Sigma-Aldrich
Acetylthiocholine chloride ≥99% (TLC), powder | 6050-81-3
Activity of Cholinesterases in Human Whole Blood Measured with Acetylthiocholine as Substrate and Ethopropazine as...
... suggested for measuring acetylcholinesterase and butyrylcholinesterase activities in human whole blood using acetylthiocholine ... E. Reiner, A. Bosak i V. Simeon-Rudolf, "Activity of Cholinesterases in Human Whole Blood Measured with Acetylthiocholine as ... Reiner E, Bosak A, Simeon-Rudolf V. Activity of Cholinesterases in Human Whole Blood Measured with Acetylthiocholine as ... Activity of Cholinesterases in Human Whole Blood Measured with Acetylthiocholine as Substrate and Ethopropazine as Selective ...
Sensors | Free Full-Text | Critical Evaluation of Acetylthiocholine Iodide and Acetylthiocholine Chloride as Substrates for...
We investigate the possibility of using acetylthiocholine iodide as pseudosubstrate for amperometric detection. Our ... is quantified by the oxidation of the thiocholine that is produced enzymatically by the hydrolysis of the acetylthiocholine ... investigation demonstrates that operational conditions for any amperometric biosensor that use acetylthiocholine iodide must be ... Keywords: acetylthiocholine iodide; acetylthiocholine chloride; amperometry; acetylcholinesterase acetylthiocholine iodide; ...
AID 1097367 - Inhibition of AChE in po dosed Charles Foster albino Rattus norvegicus (rat) assessed as hydrolysis of...
AID 1085535 - Inhibition of Electrophorus electricus (electric eel) acetylcholinesterase (AChE) using acetylthiocholine iodide...
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Acetylcholinesterase sensor based on screen-printed carbon electrode modified with prussian blue | SpringerLink
Sensors | Free Full-Text | Nanomaterials - Acetylcholinesterase Enzyme Matrices for Organophosphorus Pesticides Electrochemical...
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Distribution of cholinesterases in insects. - PubMed - NCBI
In general, acetylthiocholine was hydrolysed slightly more rapidly by insect cholinesterases. A unique cholinesterase was found ... Kinetic data indicate that acetylthiocholine has a greater affinity than does phenyl thioacetate for a variety of enzyme ... The utility of histochemistry in conjunction with in vitro methods is discussed.The substrates acetylthiocholine and phenyl ... Ultrastructural evidence shows that cholinesterases that hydrolyse acetylthiocholine are membrane-bound. Phenyl thioacetate was ...
A Guided Materials Screening Approach for Developing Quantitative Sol-gel Derived Protein Microarrays | Protocol
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Nickel in Soil Modifies Sensitivity to Diazinon Measured by the Activity of Acetylcholinesterase, Catalase, and Glutathione S...
Activity is expressed as nmol acetylthiocholine min−1 mg−1 protein.. The catalase (CAT) activity was determined by monitoring ... The principle of this method is the hydrolysis of acetylthiocholine iodide by AChE, and spectrophotometrical detection (410 nm ... Acetylcholinesterase (AChE) activity (nmol hydrolysed acetylthiocholine iodide*min−1*mg−1 protein), S-glutathione transferase ( ... of the yellow product of the reaction of acetylthiocholine with DTNB in adequate milieu. ...
AChR Activators | SCBT - Santa Cruz Biotechnology
Plus it
... acetylthiocholine (ASCh; □), or choline (chol; ▴). Log EC50 values and Hill coefficients (± S.E.M.) are provided in Table 2, ... and perhaps acetylthiocholine; and very weak potency for choline (Fig. 7, Table 2). Lobeline (not shown) and succinylcholine ... 100 μM acetylthiocholine (75%) » 3.8 mM (estimated) choline (22% at 1 mM). Self-inhibitory IC50 values were also determined for ... 7.1 μM acetylthiocholine » 290 μM choline. Lobeline (IC50 = 76 nM) had ligand binding competition potency greater than any ...
Molecules | Free Full-Text | Why is Aged Acetylcholinesterase So Difficult to Reactivate? | HTML
... acetylthio)choline. J. Am. Chem. Soc. 2000, 122, 2981-2987. [Google Scholar] [CrossRef] ... Consider the acylation transition state for AChE catalyzed hydrolysis of acetylthiocholine (ATCh). By measuring β-deuterium ... A secondary isotope effect study of equine serum butyrylcholinesterase-catalyzed hydrolysis of acetylthiocholine. Chem. Biol. ... The reactant state for substrate-activated turnover of acetylthiocholine by butyrylcholinesterase is a tetrahedral intermediate ...
Zeitschrift für Naturforschung C Volume 57 Issue 11-12 (2002)
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Experimental Applications | Springer for Research & Development
Spectral Database Index:
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ACHE Recombinant Mouse Protein, His Tag, Invitrogen™ Sino Biological™
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Hetero compounds with composition C H N O S
Hydrolysis of Acetylthiocholine4
- Hydrolysis of acetylthiocholine by AChE shows true first-order kinetics with a turnover of 64,000 sec -1 . (caymanchem.com)
- Non-enzymatic hydrolysis of acetylthiocholine in buffer is essentially absent. (caymanchem.com)
- The (R)- and (S)-acetates also act as nonstereoselective inhibitors of the enzyme-induced hydrolysis of acetylthiocholine. (srce.hr)
- In this work, we detected AChE at the interface between stele and cortex of the mesocotyl of Zea mays by measuring hydrolysis of acetylthiocholine and by liberation of labeled acetate from [1- 14 C]ACh. (plantphysiol.org)
Acetylcholinesterase5
- A procedure is suggested for measuring acetylcholinesterase and butyrylcholinesterase activities in human whole blood using acetylthiocholine as a substrate and ethopropazine as a selective inhibitor of butyrylcholinesterase. (srce.hr)
- Bucur M-P, Bucur B, Radu G-L. Critical Evaluation of Acetylthiocholine Iodide and Acetylthiocholine Chloride as Substrates for Amperometric Biosensors Based on Acetylcholinesterase. (mdpi.com)
- Recombinant P. papatasi AChE1 was expressed in the baculovirus system and characterized as an insect acetylcholinesterase with substrate preference for acetylthiocholine and inhibition at high substrate concentration. (usda.gov)
- Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway. (semanticscholar.org)
- Native polyacrylamide gel electrophoresis (PAGE) analysis of extracts solubilized with Triton X-100 from heads and decapitated bodies revealed five major esterase bands and an acetylcholinesterase (AChE) band with a high capability of hydrolyzing α-naphthyl butyrate and acetylthiocholine, respectively. (unl.edu)
ACHE5
- AChE assays are developed with Ellman's Reagent , which contains acetylthiocholine as the substrate. (caymanchem.com)
- The substrate, acetylthiocholine is hydrolyzed into thiocholine and acetate by the enzyme AChE. (pharmatutor.org)
- Here, we present the crystal structures of Torpedo californica AChE complexed with the substrate acetylthiocholine, the product thiocholine and a nonhydrolysable substrate analogue. (proteopedia.org)
- AChE activity was determined spectrophotometrically using acetylthiocholine iodide as substrate in the erythrocyte and liver. (trjfas.org)
- AE-2 partially inhibited the rate of hydrolysis of the charged substrate acetylthiocholine by FBS AChE, whereas it increased the rate of hydrolysis of the neutral substrate indophenyl acetate. (aspetjournals.org)
Acetylcholine4
- Acetylthiocholine is an acetylcholine analog used in scientific research. (wikipedia.org)
- Acetylthiocholine chloride has been used to determine the acetylcholine esterase activity of semen exosomes (SE). (sigmaaldrich.com)
- The Enzymatic Hydrolysis of the beta-Methyl Derivatives of Acetylcholine and Acetylthiocholine. (actachemscand.dk)
- and Zheng, Wencui, "Theoretical Investigations of Acetylcholine (ACh) and Acetylthiocholine (ATCh) Using ab Initio and Effective Fragment Potential Methods" (2004). (iastate.edu)
Substrates3
- The utility of histochemistry in conjunction with in vitro methods is discussed.The substrates acetylthiocholine and phenyl thioacetate were utilized in demonstrating cholinesterase. (nih.gov)
- Substrates for the assay included acetylthiocholine (ATC) and butyrylthiocholine (BTC). (cdc.gov)
- Under the conditions of chronic anthropogenic pollution, the cholinesterase of the mussel hemolymph loses its ability to hydrolyze substrates other than acetylthiocholine. (deepdyve.com)
Thiocholine3
- The analytical signal is quantified by the oxidation of the thiocholine that is produced enzymatically by the hydrolysis of the acetylthiocholine pseudosubstrate. (mdpi.com)
- The thiocholine esters, acetylthiocholine, butyrylthiocholine and acetyl-β-methylthiocholine, were considerably more potent than was ACh. (aspetjournals.org)
- The substrate used in the assay system is acetylthiocholine iodide, the ester of thiocholine and acetic acid. (pharmatutor.org)
Assay1
- test results obtained using a conversion factor which standardizes to the acetylthiocholine assay at 25°C. (sbmflab.org)
Enzyme2
- Kinetic data indicate that acetylthiocholine has a greater affinity than does phenyl thioacetate for a variety of enzyme sources. (nih.gov)
- The amount of enzyme causing the hydrolysis of one micromole of acetylthiocholine iodide per minute at 25 C and pH 8.0. (calzyme.com)
Butyrylthiocholine1
- In the DTNB (dithiobis nitrobenzoic acid) method, substrate sensitivity depended on the animal species - propionylthiocholine iodide (PTC) was most sensitive in horse, dog and cat serum, butyrylthiocholine iodide (BTC) and PTC were more reactive to monkey serum, and acetylthiocholine iodide (ATC) was most effective in pig and cattle serum. (eurekamag.com)
DTNB1
- The plate was sprayed with 5,5'-dithiobis(2nitrobenzoic acid) (DTNB)/acetylthiocholine iodide ( ATCI ) reagent (1mM DTNB and 1mM ATCI in 50 mM Tris-HCl, pH 8) until the silica was carefully saturated with the solvent. (thefreedictionary.com)
Hydrolyze1
- One unit will hydrolyze 1.0 μmole of acetylthiocholine iodide per min at pH 7.4 at 37°C. (creative-enzymes.com)
Cholinesterases4
- Activity of Cholinesterases in Human Whole Blood Measured with Acetylthiocholine as Substrate and Ethopropazine as. (srce.hr)
- Activity of Cholinesterases in Human Whole Blood Measured with Acetylthiocholine as Substrate and Ethopropazine as Selective Inhibitor of Plasma Butytylcholinesterase', Arhiv za higijenu rada i toksikologiju , 55(1), str. (srce.hr)
- In general, acetylthiocholine was hydrolysed slightly more rapidly by insect cholinesterases. (nih.gov)
- Ultrastructural evidence shows that cholinesterases that hydrolyse acetylthiocholine are membrane-bound. (nih.gov)
Protein1
- The results to be expressed as nmols of acetylthiocholine iodide hydrolyzed/min/mg protein. (pharmatutor.org)
Detection1
- We investigate the possibility of using acetylthiocholine iodide as pseudosubstrate for amperometric detection. (mdpi.com)
Product1
- These structures provide a series of static snapshots of the substrate en route to the active site and identify, for the first time, binding of substrate and product at both the peripheral and active sites. (proteopedia.org)
General1
- The disparate pH dependences for reactivation of ChE and the general base-catalyzed oximolysis of acetylthiocholine reveal that distinct reactivator ionization states are involved in the reactivation of ChE conjugates and in conferring nucleophilic reactivity of the oxime group. (elsevier.com)
Publications1
- Office for Publications of the European Union L-2985 Luxembourg EN Case No COMP/M.7435 - MERCK/ SIGMA-ALDRICH Only the English text is available and authentic. (safirazmakian.com)
IODIDE3
- 5 and 35 °C with acetylthiocholine iodide as substrate. (elsevier.com)
- 62 mM for acetylthiocholine iodide and 2. (elsevier.com)
- Post mitochondrial fractions prepared from whole body homogenates were used to measure esterase activity with the following 5 substrates: p-nitrophenyl acetate ( PNPA), (-naphthyl acetate (ANA), phenyl acetate (pHA), carboxylic esterase activity and acetylthiocholine iodide (Ach! (ac.zw)