The benzoic acid ester of choline.
A local anesthetic of the amide type now generally used for surface anesthesia. It is one of the most potent and toxic of the long-acting local anesthetics and its parenteral use is restricted to spinal anesthesia. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1006)
A mercaptocholine used as a reagent for the determination of CHOLINESTERASES. It also serves as a highly selective nerve stain.
Cholinesterases are a group of enzymes that catalyze the hydrolysis of acetylcholine and other choline esters, playing crucial roles in the termination of impulse transmission at cholinergic synapses and neuro-muscular junctions, and in the metabolism of certain drugs and toxic substances.
A sulfur-containing analog of butyrylcholine which is hydrolyzed by butyrylcholinesterase to butyrate and thiocholine. It is used as a reagent in the determination of butyrylcholinesterase activity.
An aspect of cholinesterase (EC 3.1.1.8).
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
A quaternary skeletal muscle relaxant usually used in the form of its bromide, chloride, or iodide. It is a depolarizing relaxant, acting in about 30 seconds and with a duration of effect averaging three to five minutes. Succinylcholine is used in surgical, anesthetic, and other procedures in which a brief period of muscle relaxation is called for.
Drugs that block nerve conduction when applied locally to nerve tissue in appropriate concentrations. They act on any part of the nervous system and on every type of nerve fiber. In contact with a nerve trunk, these anesthetics can cause both sensory and motor paralysis in the innervated area. Their action is completely reversible. (From Gilman AG, et. al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 8th ed) Nearly all local anesthetics act by reducing the tendency of voltage-dependent sodium channels to activate.
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.
The rate dynamics in chemical or physical systems.
An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and acetate. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC 3.1.1.7.
An organophosphorus compound that inhibits cholinesterase. It causes seizures and has been used as a chemical warfare agent.
Reduction of pharmacologic activity or toxicity of a drug or other foreign substance by a living system, usually by enzymatic action. It includes those metabolic transformations that make the substance more soluble for faster renal excretion.

Probing the structure of the nicotinic acetylcholine receptor with 4-benzoylbenzoylcholine, a novel photoaffinity competitive antagonist. (1/8)

[(3)H]4-Benzoylbenzoylcholine (Bz(2)choline) was synthesized as a photoaffinity probe for the Torpedo nicotinic acetylcholine receptor (nAChR). [(3)H]Bz(2)choline acts as an nAChR competitive antagonist and binds at equilibrium with the same affinity (K(D) = 1.4 microm) to both agonist sites. Irradiation at 320 nm of nAChR-rich membranes equilibrated with [(3)H]Bz(2)choline results in the covalent incorporation of [(3)H]Bz(2)choline into the nAChR gamma- and delta-subunits that is inhibitable by agonist, with little specific incorporation in the alpha-subunits. To identify the sites of photoincorporation, gamma- and delta-subunits, isolated from nAChR-rich membranes photolabeled with [(3)H]Bz(2)choline, were digested enzymatically, and the labeled fragments were isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and/or reversed-phase high performance liquid chromatography. For the gamma-subunit, Staphylococcus aureus V8 protease produced a specifically labeled peptide beginning at gammaVal-102, whereas for the delta-subunit, endoproteinase Asp-N produced a labeled peptide beginning at deltaAsp-99. Amino-terminal sequence analysis identified the homologous residues gammaLeu-109 and deltaLeu-111 as the primary sites of [(3)H]Bz(2)choline photoincorporation. This is the first identification by affinity labeling of non-reactive amino acids within the acetylcholine-binding sites, and these results establish that when choline esters of benzoic acid are bound to the nAChR agonist sites, the para substituent is selectively oriented toward and in proximity to amino acids gammaLeu-109/deltaLeu-111.  (+info)

Rate-determining step of butyrylcholinesterase-catalyzed hydrolysis of benzoylcholine and benzoylthiocholine. Volumetric study of wild-type and D70G mutant behavior. (2/8)

The rate-limiting step for hydrolysis of the positively charged oxoester benzoylcholine (BzCh) by human butyrylcholinesterase (BuChE) is deacylation (k(3)), whereas it is acylation (k(2)) for hydrolysis of the homologous thioester benzoylthiocholine (BzSCh). Steady-state hydrolysis of BzCh and BzSCh by wild-type BuChE and its peripheral anionic site mutant D70G was investigated at different hydrostatic pressures, which allowed determination of volume changes associated with substrate binding, and the activation volumes for the chemical steps. A differential nonlinear pressure-dependence of the catalytic parameters for hydrolysis of both substrates by both enzymes was shown. Nonlinearity of the plots may be explained in terms of compressibility changes or rate-limiting changes. To distinguish between these two possibilities, enzyme phosphorylation by diisopropylfluorophosphate (DFP) in the presence of substrate (BzSCh) under pressure was studied. There was no pressure dependence of volume changes for DFP binding or for phosphorylation of either wild-type or D70G. Analysis of the pressure dependence for steady-state hydrolysis of substrates, and for phosphorylation by DFP provided evidence that no enzyme compressibility changes occurred during the catalyzed reactions. Thus, the nonlinear pressure dependence of substrate hydrolysis reflects changes in the rate-limiting step with pressure. Change in rate-determining step occurred at a pressure of 100 MPa for hydrolysis of BzCh by wild-type and at 75 MPa for D70G. For hydrolysis of BzSCh the change occurred at higher pressures because k(2) << k(3) at atmospheric pressure for this substrate. Elementary volume change contributions upon initial binding, productive binding, acylation and deacylation were calculated from the pressure differentiation of kinetic constants. This analysis shed light on the molecular events taking place along the hydrolysis pathways of BzCh and BzSCh by wild-type BuChE and the D70G mutant. In addition, volume change differences between wild-type and D70G provided new evidence that residue D70 in the peripheral site controls hydration of the active site gorge and the dynamics of the water molecule network during catalysis. Finally, a steady-state kinetic study of the oxyanion hole mutant (G117H) showed that substitution of the ethereal sulfur for oxygen in the substrate alters the final adjustment of substrate in the active site and stabilization of the acylation transition state.  (+info)

Hydrolysis of oxo- and thio-esters by human butyrylcholinesterase. (3/8)

Catalytic parameters of human butyrylcholinesterase (BuChE) for hydrolysis of homologous pairs of oxo-esters and thio-esters were compared. Substrates were positively charged (benzoylcholine versus benzoylthiocholine) and neutral (phenylacetate versus phenylthioacetate). In addition to wild-type BuChE, enzymes containing mutations were used. Single mutants at positions: G117, a key residue in the oxyanion hole, and D70, the main component of the peripheral anionic site were tested. Double mutants containing G117H and mutations on residues of the oxyanion hole (G115, A199), or the pi-cation binding site (W82), or residue E197 that is involved in stabilization of tetrahedral intermediates were also studied. A mathematical analysis was used to compare data for BuChE-catalyzed hydrolysis of various pairs of oxo-esters and thio-esters and to determine the rate-limiting step of catalysis for each substrate. The interest and limitation of this method is discussed. Molecular docking was used to analyze how the mutations could have altered the binding of the oxo-ester or the thio-ester. Results indicate that substitution of the ethereal oxygen for sulfur in substrates may alter the adjustment of substrate in the active site and stabilization of the transition-state for acylation. This affects the k2/k3 ratio and, in turn, controls the rate-limiting step of the hydrolytic reaction. Stabilization of the transition state is modulated both by the alcohol and acyl moieties of substrate. Interaction of these groups with the ethereal hetero-atom can have a neutral, an additive or an antagonistic effect on transition state stabilization, depending on their molecular structure, size and enantiomeric configuration.  (+info)

Cholinesterases from flounder muscle. Purification and characterization of glycosyl-phosphatidylinositol-anchored and collagen-tailed forms differing in substrate specificity. (4/8)

Flounder (Platichthys flesus) muscle contains two types of cholinesterases, that differ in molecular form and in substrate specificity. Both enzymes were purified by affinity chromatography. About 8% of cholinesterase activity could be attributed to collagen-tailed asymmetric acetylcholinesterase sedimenting at 17S, 13S and 9S, which showed catalytic properties of a true acetylcholinesterase. 92% of cholinesterase activity corresponded to an amphiphilic dimeric enzyme sedimenting at 6S in the presence of Triton X-100. Treatment with phospholipase C yielded a hydrophilic form and uncovered an epitope called the cross-reacting determinant, which is found in the hydrophilic form of a number of glycosyl-phosphatidylinositol-anchored proteins. This enzyme showed catalytic properties intermediate to those of acetylcholinesterase and butyrylcholinesterase. It hydrolyzed acetylthiocholine, propionylthiocholine, butyrylthiocholine and benzoylthiocholine. The Km and the maximal velocity decreased with the length and hydrophobicity of the acyl chain. At high substrate concentrations the enzyme was inhibited. The p(IC50) values for BW284C51 and ethopropazine were between those found for acetylcholinesterase and butylcholinesterase. For purified detergent-soluble cholinesterase a specific activity of 8000 IU/mg protein, a turnover number of 2.8 x 10(7) h-1, and 1 active site/subunit were determined.  (+info)

Comparison of a commercially available assay system with two reference methods for the determination of plasma cholinesterase variants. (5/8)

For assaying plasma cholinesterase (EC 3.1.1.8) activity and phenotyping by means of dibucaine inhibition, we have compared a commercially available kit, in which butyrylthiocholine is used as substrate, with two reference methods, one using benzoylcholine and the other propionylthiocholine. With 50 different samples of three of the most common genetic variants, we could clearly differentiate the variants with benzoylcholine and dibucaine, whereas there was some overlap of the E1uE1u and E1uE1a phenotypes with the other two substrates at 30 degrees C. The phenotypes were better differentiated at 25 degrees C, and in our hands the use of butyrylthiocholine was preferable to propionylthiocholine for phenotyping with dibucaine. The affinity of the usual and atypical homozygotes for fluoride with butyrylthiocholine gave an inverted response to the affinity of these variants for the anion with benzoylcholine. We suggest that this may be explained by the role of the chromogen or its products in the assay procedure with the thiocholine substrate.  (+info)

Rate assay for determination of serum pseudo-cholinesterase activity. (6/8)

A simple and reproducible method for the determination of serum pseudo-cholinesterase activity was developed by making use of a stable substrate, p-hydroxybenzoylcholine, with p-hydroxybenzoate hydroxylase as a linked enzyme. The method is based on spectrophotometric measurement of the decrease of NADPH. p-Hydroxybenzoate released from p-hydroxybenzoylcholine is hydroxylated by the action of p-hydroxybenzoate hydroxylase in the presence of NADPH and O2 to produce 3,4-dihydroxybenzoate and NADP+. This method is superior to the conventional methods in that this substrate is extremely stable up to pH 9.0, which is close to the optimum pH for the assay (pH 8.0). Serum interference was resolved by the use of p-hydroxybenzoate hydroxylase as a linked enzyme. The Km value of pseudocholinesterase for p-hydroxybenzoylcholine is 1 X 10(-5) M. The results of our method and Garry's method (Clin. Chem. 11, 91-96, 1965) correlated well (r = 0.962). The within-run and between-run C.V. values were 2.1 and 2.7, respectively.  (+info)

Is serum cholinesterase activity a predictor of succinyl choline sensitivity? An assessment of four methods. (7/8)

Four methods for measuring serum cholinesterase activity have been applied to sera of normal individuals and of patients shown to be sensitive to short-acting muscle relaxants of the succinyldicholine type. They have been assessed according to their ability to differentiate between sensitive and insensitive individuals on the basis of enzyme activity measurements alone. The method described, based upon that of Dietz et al. [Clin. Chem. 19, 1309 (1973)], in which propionylthiocholine is used as substrate, is best for this purpose, being capable of identifying over 90% of affected individuals with no false positives. Acetylcholine and butyrylthiocholine are slightly inferior substrates in this respect, and benzoylcholine gives little useful information.  (+info)

Kinetics of local anesthetic esters and the effects of adjuvant drugs on 2-chloroprocaine hydrolysis. (8/8)

A rapid, reliable method for the determination of 2-chloroprocaine in serum was developed. The method, using double-beam ultraviolet spectroscopy, provides rapid, accurate analysis of 2-chloroprocaine in the range of 5.5 to 111 microM (1.5--30 microgram/ml), as documented by comparison with the accepted gas chromatographic procedure. The contribution of 4-amino-2-chlorobenzoic acid, the principal metabolite of 2-chloroprocaine, to the total absorbance at 300 nm was examined and found to be negligible. Using the ultraviolet spectrophotometric method, values of the Michaelis-Menton constant (Km) and maximal reaction velocity (Vmax) for hydrolysis of procaine and 2-chloroprocaine by homozygous typical, heterozygous, and homozygous atypical plasma cholinesterase were determined. The Kms for the three genotypes were 5.0, 6.2, and 14.7 microM, respectively, for procaine, and 8.2, 17, and 103 microM, respectively for 2-chloroprocaine. The Vmaxs for the three genotyps were similar for all esters. Vmax for procaine was 18.6 +/- 0.9 nmol/min/ml serum, while Vmax for 2-chloroprocaine was 98.4 +/- 2.1 nmol/min/ml serum. At high concentrations, 2-chloroprocaine acts as an inhibitor of its hydrolysis. The inhibitory effects of lidocaine, bupivacaine, neostigmine, and succinyldicholine on 2-chloroprocaine hydrolysis for homozygous typical and atypical variants, respectively, were studied. Competitive inhibition was demonstrated for all four drugs. However, at clinically significant concentrations, only neostigmine and bupivacaine produced high degrees of inhibition. The competitive inhibition constants (K1) for the typical and atypical variants, respectively, were 3.3 +/- 0.3 microM and 15.1 +/- 4.8 microM for neostigmine, and 4.2 +/- 0.3 microM and 36.9 +/- 9.8 microM for bupivacaine.  (+info)

Benzoylcholine, also known as benzoylcholine or physostigmine salicylate, is not a medical term commonly used to define a specific medical condition or disease. Instead, it is a chemical compound that has been used in medical research and some therapeutic applications.

Benzoylcholine is a synthetic derivative of physostigmine, a natural alkaloid found in the Calabar bean. Physostigmine is an inhibitor of acetylcholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine in the body. Benzoylcholine also acts as an inhibitor of acetylcholinesterase and has been used in research to study the cholinergic system, which is involved in various physiological processes such as memory, attention, and muscle contraction.

In clinical settings, benzoylcholine has been used as a diagnostic tool to test for myasthenia gravis, a neuromuscular disorder characterized by weakness and fatigue of the skeletal muscles. The administration of benzoylcholine in patients with myasthenia gravis can cause a transient worsening of symptoms due to the accumulation of acetylcholine at the neuromuscular junction.

It is important to note that benzoylcholine should only be used under medical supervision and its use is generally limited to research or diagnostic settings.

Dibucaine is a local anesthetic drug that is used to numb the skin or mucous membranes before medical procedures. It works by blocking the nerve signals in the area where it is applied, preventing the sensation of pain. Dibucaine is available as a topical cream, ointment, or gel, and it may also be used as an ingredient in lozenges or throat sprays to relieve sore throats.

Dibucaine has been largely replaced by other local anesthetics due to its potential for causing allergic reactions and other side effects. It is important to follow your healthcare provider's instructions carefully when using dibucaine, and to inform them of any medical conditions or medications you are taking that may interact with the drug.

Thiocholine is not a medical term per se, but it is a chemical compound that has applications in the medical and biological fields. Thiocholine is the reduced form of thiochrome, which is a derivative of vitamin B1 (thiamine). It is often used as a reagent in biochemical assays to measure the activity of acetylcholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine.

In this context, thiocholine iodide (S-[2-(hydroxyethyl)thio]ethan-1-oniuim iodide) is commonly used as a substrate for acetylcholinesterase. When the enzyme hydrolyzes thiocholine iodide, it produces thiocholine, which can be detected and quantified through its reaction with ferric chloride to form a colored complex. This assay is useful in diagnosing certain neurological conditions or monitoring the effectiveness of treatments that target the cholinergic system.

Cholinesterases are a group of enzymes that play an essential role in the nervous system by regulating the transmission of nerve impulses. They work by breaking down a type of chemical messenger called acetylcholine, which is released by nerves to transmit signals to other nerves or muscles.

There are two main types of cholinesterases: acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). AChE is found primarily in the nervous system, where it rapidly breaks down acetylcholine to terminate nerve impulses. BChE, on the other hand, is found in various tissues throughout the body, including the liver and plasma, and plays a less specific role in breaking down various substances, including some drugs and toxins.

Inhibition of cholinesterases can lead to an accumulation of acetylcholine in the synaptic cleft, which can result in excessive stimulation of nerve impulses and muscle contractions. This effect is exploited by certain medications used to treat conditions such as myasthenia gravis, Alzheimer's disease, and glaucoma, but can also be caused by exposure to certain chemicals or toxins, such as organophosphate pesticides and nerve agents.

Butyrylthiocholine is a synthetic chemical compound that is often used in scientific research, particularly in the study of enzymes and neurotransmitters. It is the substrate for the enzyme butyrylcholinesterase, which is found in the blood and helps to break down certain types of drugs and neurotransmitters.

In biochemical terms, butyrylthiocholine is a choline ester of butyric acid, with a thio (sulfur) group replacing one of the oxygen atoms in the ester linkage. This structural feature makes it an excellent substrate for butyrylcholinesterase, as the sulfur atom can form a covalent bond with the enzyme's active site, leading to rapid and specific catalysis.

It is important to note that butyrylthiocholine itself does not have any direct medical relevance, but rather serves as a tool for studying the mechanisms of enzymes and other biological processes.

Butyrylcholinesterase (BChE) is an enzyme that catalyzes the hydrolysis of esters of choline, including butyrylcholine and acetylcholine. It is found in various tissues throughout the body, including the liver, brain, and plasma. BChE plays a role in the metabolism of certain drugs and neurotransmitters, and its activity can be inhibited by certain chemicals, such as organophosphate pesticides and nerve agents. Elevated levels of BChE have been found in some neurological disorders, while decreased levels have been associated with genetic deficiencies and liver disease.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Succinylcholine is a neuromuscular blocking agent, a type of muscle relaxant used in anesthesia during surgical procedures. It works by inhibiting the transmission of nerve impulses at the neuromuscular junction, leading to temporary paralysis of skeletal muscles. This facilitates endotracheal intubation and mechanical ventilation during surgery. Succinylcholine has a rapid onset of action and is metabolized quickly, making it useful for short surgical procedures. However, its use may be associated with certain adverse effects, such as increased heart rate, muscle fasciculations, and potentially life-threatening hyperkalemia in susceptible individuals.

Local anesthetics are a type of medication that is used to block the sensation of pain in a specific area of the body. They work by temporarily numbing the nerves in that area, preventing them from transmitting pain signals to the brain. Local anesthetics can be administered through various routes, including topical application (such as creams or gels), injection (such as into the skin or tissues), or regional nerve blocks (such as epidural or spinal anesthesia).

Some common examples of local anesthetics include lidocaine, prilocaine, bupivacaine, and ropivacaine. These medications can be used for a variety of medical procedures, ranging from minor surgeries (such as dental work or skin biopsies) to more major surgeries (such as joint replacements or hernia repairs).

Local anesthetics are generally considered safe when used appropriately, but they can have side effects and potential complications. These may include allergic reactions, toxicity (if too much is administered), and nerve damage (if the medication is injected into a nerve). It's important to follow your healthcare provider's instructions carefully when using local anesthetics, and to report any unusual symptoms or side effects promptly.

Cholinesterase inhibitors are a class of drugs that work by blocking the action of cholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine in the body. By inhibiting this enzyme, the levels of acetylcholine in the brain increase, which can help to improve symptoms of cognitive decline and memory loss associated with conditions such as Alzheimer's disease and other forms of dementia.

Cholinesterase inhibitors are also used to treat other medical conditions, including myasthenia gravis, a neuromuscular disorder that causes muscle weakness, and glaucoma, a condition that affects the optic nerve and can lead to vision loss. Some examples of cholinesterase inhibitors include donepezil (Aricept), galantamine (Razadyne), and rivastigmine (Exelon).

It's important to note that while cholinesterase inhibitors can help to improve symptoms in some people with dementia, they do not cure the underlying condition or stop its progression. Side effects of these drugs may include nausea, vomiting, diarrhea, and increased salivation. In rare cases, they may also cause seizures, fainting, or cardiac arrhythmias.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Acetylcholinesterase (AChE) is an enzyme that catalyzes the hydrolysis of acetylcholine (ACh), a neurotransmitter, into choline and acetic acid. This enzyme plays a crucial role in regulating the transmission of nerve impulses across the synapse, the junction between two neurons or between a neuron and a muscle fiber.

Acetylcholinesterase is located in the synaptic cleft, the narrow gap between the presynaptic and postsynaptic membranes. When ACh is released from the presynaptic membrane and binds to receptors on the postsynaptic membrane, it triggers a response in the target cell. Acetylcholinesterase rapidly breaks down ACh, terminating its action and allowing for rapid cycling of neurotransmission.

Inhibition of acetylcholinesterase leads to an accumulation of ACh in the synaptic cleft, prolonging its effects on the postsynaptic membrane. This can result in excessive stimulation of cholinergic receptors and overactivation of the cholinergic system, which may cause a range of symptoms, including muscle weakness, fasciculations, sweating, salivation, lacrimation, urination, defecation, bradycardia, and bronchoconstriction.

Acetylcholinesterase inhibitors are used in the treatment of various medical conditions, such as Alzheimer's disease, myasthenia gravis, and glaucoma. However, they can also be used as chemical weapons, such as nerve agents, due to their ability to disrupt the nervous system and cause severe toxicity.

Soman is a chemical compound with the formula (CH3)2(C=O)N(CH2)4SH. It is a potent nerve agent, a type of organic compound that can cause death by interfering with the nervous system's ability to regulate muscle movement. Soman is an odorless, colorless liquid that evaporates slowly at room temperature and is therefore classified as a "v-type" or "volatile" nerve agent. It is considered to be one of the most toxic substances known. Exposure to soman can occur through inhalation, skin contact, or ingestion, and it can cause a range of symptoms including nausea, seizures, respiratory failure, and death.

Metabolic detoxification, in the context of drugs, refers to the series of biochemical processes that the body undergoes to transform drugs or other xenobiotics into water-soluble compounds so they can be excreted. This process typically involves two phases:

1. Phase I Detoxification: In this phase, enzymes such as cytochrome P450 oxidases introduce functional groups into the drug molecule, making it more polar and reactive. This can result in the formation of metabolites that are less active than the parent compound or, in some cases, more toxic.

2. Phase II Detoxification: In this phase, enzymes such as glutathione S-transferases, UDP-glucuronosyltransferases, and sulfotransferases conjugate these polar and reactive metabolites with endogenous molecules like glutathione, glucuronic acid, or sulfate. This further increases the water solubility of the compound, allowing it to be excreted by the kidneys or bile.

It's important to note that while these processes are essential for eliminating drugs and other harmful substances from the body, they can also produce reactive metabolites that may cause damage to cells and tissues if not properly regulated. Therefore, maintaining a balance in the activity of these detoxification enzymes is crucial for overall health and well-being.

Km for the uncharged ester, o-nitrophenylbutyrate, was 0.14 mM for both enzymes, whereas Km for benzoylcholine was 0.005 mM for ... The turnover numbers of usual and atypical cholinesterases were the same: 15,000 mumol of benzoylcholine hydrolyzed/min/mumol ...
... benzoylcholine, and succinylcholine, and for aromatic esters (e.g., procaine, chloroprocaine, tetracaine). Normal PCE is ...
... benzoylcholine MeSH D02.241.223.100.215 - bumetanide MeSH D02.241.223.100.275 - dicamba MeSH D02.241.223.100.360 - hexobendine ... benzoylcholine MeSH D02.092.877.883.333.115 - carbachol MeSH D02.092.877.883.333.130 - cytidine diphosphate choline MeSH ... benzoylcholine MeSH D02.675.276.232.115 - carbachol MeSH D02.675.276.232.130 - cytidine diphosphate choline MeSH D02.675. ...
"Benzoylcholine" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Benzoylcholine" by people in this website by year, and whether ... Below are the most recent publications written about "Benzoylcholine" by people in Profiles. ... "Benzoylcholine" was a major or minor topic of these publications. To see the data from this visualization as text, click here. ...
Km for the uncharged ester, o-nitrophenylbutyrate, was 0.14 mM for both enzymes, whereas Km for benzoylcholine was 0.005 mM for ... The turnover numbers of usual and atypical cholinesterases were the same: 15,000 mumol of benzoylcholine hydrolyzed/min/mumol ...
below the median level for the sample as a whole (1.09 μmoles benzoylcholine per minute per mL serum). Prevalence odds ratios ( ... Phenotype was determined by measuring serum enzyme activity with benzoylcholine in Na/K phosphate buffer, as previously ...
Email me at this address if my answer is selected or commented on:Email me if my answer is selected or commented on ...
Substrates and inhibitors. Substrates were N-methylindoxyl acetate (NMIA), butyrylthiocholine (BuSCh), benzoylcholine (BzCh), ... The enzyme is rat BuChE hydrolyzing an N-alkyl derivative of benzoylcholine (N-(2-benzoyloxyethyl)-alkyldimethyl ammonium ... and benzoylcholine (BzCh) [16]. Hysteresis of human and rat BuChE with BzCh as a substrate was even more complex, showing ... benzoylcholine; BzSCh, benzoylthiocholine; CBDP, cresyl saligenin phosphate; ChE, cholinesterase; MNPCC, N-methyl-N-(2- ...
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Benzoylcholine was shown to be a poor substrate of AChE, and steady-state kinetics showed a sudden inhibition at high ...
G117H was still able to hydrolyze butyrylthiocholine, benzoylcholine, and o-nitrophenyl butyrate, but in addition it had ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
This graph shows the total number of publications written about "Chlorobenzoates" by people in this website by year, and whether "Chlorobenzoates" was a major or minor topic of these publications ...
Benzoylcholine. *Carbachol. *Cytidine Diphosphate Choline. *Phosphorylcholine. *Platelet Activating Factor. * ...
Mathieu LN, Larkins E, Akinboro O, Roy P, Amatya AK, Fiero MH, Mishra-Kalyani PS, Helms WS, Myers CE, Skinner AM, Aungst S, Jin R, Zhao H, Xia H, Zirkelbach JF, Bi Y, Li Y, Liu J, Grimstein M, Zhang X, Woods S, Reece K, Abukhdeir AM, Ghosh S, Philip R, Tang S, Goldberg KB, Pazdur R, Beaver JA, Singh H. FDA Approval Summary: Capmatinib and Tepotinib for the Treatment of Metastatic NSCLC Harboring MET Exon 14 Skipping Mutations or Alterations. Clin Cancer Res. 2022 01 15; 28(2):249-254 ...
Benzoylcholine [D02.092.877.883.333.100] * Carbachol [D02.092.877.883.333.115] * Cytidine Diphosphate Choline [D02.092.877.883. ...
benzoylcholine (Sigma-Aldrich) in a protocol modified from published methods42,43 for a reaction volume of 200. μ. L. . ... Benzoylcholine assays were conducted in ultraviolet-transparent microplates (Greiner Bio); the reactions were monitored using ...
... and benzoylcholine -BeChE- as substrates. The study population consisted of intensive agriculture workers regularly exposed to ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
Benzoylcholine Preferred Term Term UI T004594. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ... Benzoylcholine Preferred Concept UI. M0002380. Registry Number. 2208-04-0. Scope Note. The benzoic acid ester of choline.. ... Benzoylcholine. Tree Number(s). D02.092.877.883.333.100. D02.241.223.100.141. D02.455.426.559.389.127.141. D02.675.276.232.100 ...
Benzoylcholine Preferred Term Term UI T004594. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ... Benzoylcholine Preferred Concept UI. M0002380. Registry Number. 2208-04-0. Scope Note. The benzoic acid ester of choline.. ... Benzoylcholine. Tree Number(s). D02.092.877.883.333.100. D02.241.223.100.141. D02.455.426.559.389.127.141. D02.675.276.232.100 ...
O-Benzoyl-choline Tree number(s):. D02.092.877.883.333.100. D02.241.223.100.141. D02.455.426.559.389.127.141. D02.675.276.232. ...
Peroxide N0000170233 Benzoylarginine Nitroanilide N0000170229 Benzoylarginine-2-Naphthylamide N0000166652 Benzoylcholine ...
... benzoylcholine esters. PMID- 5165607 TI - Potential antineoplastics. 8. Synthesis and pharmacology of 6-methyl-2-thio-5 ...
Steady-state kinetic parameters for hydrolysis of butyrylthiocholine, benzoylcholine, succinyldithiocholine, and o-nitrophenyl ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
D2.455.426.559.389.127.133 Benzoylcholine D2.241.223.100.156 D2.241.223.100.141 D2.455.426.559.389.127.141 Bermuda Z1.295.390 ...
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Benzoylcholine Benzphetamine Benztropine Benzydamine Benzyl Alcohol Benzyl Alcohols Benzyl Compounds Benzyl Viologen ...
  • Differently, the enzyme showed substrate inhibition with benzoylcholine (BzCh) and a k(cat)/K-m value of 21,190 was found. (hacettepe.edu.tr)
  • G117H was still able to hydrolyze butyrylthiocholine, benzoylcholine, and o-nitrophenyl butyrate, but in addition it had acquired the ability to hydrolyze the antiglaucoma drug echothiophate and the pesticide paraoxon. (inra.fr)