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> Chemicals & Drugs > Amino Acid > Butyrylcholinesterase

Butyrylcholinesterase

Butyrylcholinesterase is an enzyme that catalyzes the hydrolysis of butyrylcholine and other choline esters.
It is found in various tissues, including the liver, pancreas, and plasma.
Butyrylcholinesterase plays a role in the metabolism of certain drugs and may have a protective function against organophosphate poisoning.
Reseraching this enzyme can provide insights into its biological functions and potential therapeutic applications.

Most cited protocols related to «Butyrylcholinesterase»

1
Liver Cirrhosis Screening Protocol
Cited 9 times
The study included 201 consecutive patients with liver cirrhosis admitted to two Liver Units of university/primary hospitals in Southern Italy, between the period from October 2004 to June 2007 who fulfilled the following criteria: patients' willingness to undergo previously established screening; endoscopic, US and laboratory examinations performed within four weeks of each other; prospective follow-up for a minimum period of 6 months.
Of initial patients, 26 were kept out because their US and laboratory examinations had been previously performed in different centres. Fourteen patients, who had undergone endoscopic esophageal variceal ligation therapy, and eight who had received beta-blockers before US imaging, were also excluded from the study because prior treatment might have caused a change in lesion features.
The remaining 153 patients formed the study population (85 males) whose age ranged from 31 to 85 years (median age 66 years). Chronic liver damage in these patients was caused by hepatitis B (n = 9), hepatitis C (n = 114), alcohol abuse (n = 20) or unknown etiology, likely NonAlcoholic Steato Hepatitis (NASH), (n = 8). Ninety two patients had compensated cirrhosis of the liver. For 121 patients, the diagnosis of cirrhosis was established by contextual clinical (spider nevi, organomegaly) laboratory (low total cholesterol and pseudocholinesterase levels, reduced white blood cell count, globulin/albumin ratio > 1), antecedent imaging data and for 32 patients by biopsy. The non-invasive assessment of liver cirrhosis was blindly performed de novo to all patients by radiologists on the basis of US/US-doppler examinations (coarse echo-texture, nodularity presence, increased caudate/right lobe ratio, hypertrophy of the left lobe, characterized by a rounded inferior marginal edge, and portal vein enlargement with decreased flow velocity, absence of a normal doppler waveform, hepatofugal flow). No evidence of hepatocellular carcinoma at the first hepatic decompensation was detected. Renal insufficiency was properly excluded.
Tarantino G., Citro V., Esposito P., Giaquinto S., de Leone A., Milan G., Tripodi F.S., Cirillo M, & Lobello R. (2009). Blood ammonia levels in liver cirrhosis: a clue for the presence of portosystemic collateral veins. BMC Gastroenterology, 9, 21.
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Publication 2009
Abuse, Alcohol Adrenergic beta-Antagonists Albumins Biopsy Butyrylcholinesterase Cholesterol Diagnosis ECHO protocol Endoscopy Globulins Hepatitis Hepatitis B Hepatitis C virus Hepatocellular Carcinomas Hypertrophy Leukocyte Count Ligation Liver Liver Cirrhosis Males Nevus Patients Physical Examination Radiologist Renal Insufficiency Spiders Ultrasounds, Doppler Veins Veins, Portal
2
Pesticide Exposure in Flower-Worker Families
Cited 7 times

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Publication 2012
Acetylcholinesterase Adult Biological Assay BLOOD Buttocks Butyrylcholinesterase Child Family Member Fingers Head Heel Hemoglobin Households Microtubule-Associated Proteins Occupational Exposure Pain Parent Perimetry Pesticides Physical Examination Residency Scapula Workers
3
Hepatitis Fibrosis Biomarker Evaluation
Cited 6 times
Patients with chronic hepatitis were enrolled at Nagoya City University Hospital and Hokkaido University Hospital. Healthy volunteers as the controls were randomly selected in Nagoya City University Hospital (70 individuals) and AIST (48 individuals). The institutional ethics committees at Nagoya City University Hospital, Hokkaido University Hospital, and AIST approved this study, and informed consent for the use of their clinical specimens was obtained from all participants before the collection. In addition, we used 1,000 serum samples from virus-negative Caucasians as the normal population, which were purchased from Complex Antibodies Inc. (Fort Lauderdale, FL) and collected under IRB-approved collection protocols. Fibrosis was graded in the patients according to the histological activity index (HAI) using biopsy or surgical specimens. Biopsy specimens were classified as follows: F0, no fibrosis; F1, portal fibrosis without septa; F2, few septa; F3, numerous septa without cirrhosis; and F4, cirrhosis. The three diagnostic targets in this study were defined as significant fibrosis: F2+F3+F4; severe fibrosis: F3+F4; and cirrhosis: F4. Hepatic inflammation was also assessed according to the HAI, as follows: A0, no activity; A1, mild activity; A2, moderate activity; and A3, severe activity. Cirrhosis was confirmed by ultrasonography (coarse liver architecture, nodular liver surface, and blunt liver edges), evidence of hypersplenism (splenomegaly on ultrasonography) and/or a platelet count of < 100,000/mm3. Virological responses during PEG-interferon-α and ribavirin therapy were defined as follows5 (link): SVR, absence of HCV RNA from serum 24 weeks following discontinuation of therapy; nonresponder, failure to clear HCV RNA from serum after 24 weeks of therapy; relapse, reappearance of HCV RNA in serum after therapy was discontinued. For all patients, age and sex were recorded and serum levels of the following were analyzed: aspartate aminotransferase (AST), alanine aminotransferase (ALT), γ-glutamyltransferase (GGT), total bilirubin, albumin, cholinesterase, total cholesterol, platelet count (PLT), hyaluronic acid (HA). The FIB-4 index was calculated as follows: [age (years) × AST (U/L)]/[platelets (109/L) × ALT (U/L)1/2]26 (link). Fibrosis-specific glyco-alteration of α1-acid glycoprotein was determined by lectin–antibody sandwich immunoassays with a combination of three lectins (Datura stramonium agglutinin (DSA), Maackia amurensis leukoagglutinin (MAL), and Aspergillus oryzae lectin (AOL))16 (link). All assays used an automated chemiluminescence enzyme immunoassay system (HISCL-2000i; Sysmex Co., Kobe, Japan)18 (link).
Kuno A., Ikehara Y., Tanaka Y., Ito K., Matsuda A., Sekiya S., Hige S., Sakamoto M., Kage M., Mizokami M, & Narimatsu H. (2013). A serum “sweet-doughnut” protein facilitates fibrosis evaluation and therapy assessment in patients with viral hepatitis. Scientific Reports, 3, 1065.
Publication 2013
Acids Agglutinins Albumins Antibodies Aspartate Transaminase Aspergillus oryzae Bilirubin Biological Assay Biopsy Blood Platelets Butyrylcholinesterase Caucasoid Races Chemiluminescent Assays Cholesterol D-Alanine Transaminase Enzymes Fibrosis Glycoproteins Healthy Volunteers Hepatitis, Chronic Hyaluronic acid Hypersplenism Immunoassay Immunoglobulins Inflammation Institutional Ethics Committees Interferon-alpha Jimsonweed Lectin Liver Liver Cirrhosis Maackia amurensis leukoagglutinin Operative Surgical Procedures Patients Platelet Counts, Blood Relapse Ribavirin Serum Tests, Diagnostic Therapeutics Ultrasonography Virus
4
Homology Modeling of Human Thyroid Peroxidase
Cited 5 times
Template sequences were selected by querying the TPO protein sequence against the Protein Databank (PDB) using the NCBI BLAST web server (http://blast.ncbi.nlm.nih.gov/Blast.cgi). The MPO-like, EGF-like, and CCP-like domains were modelled using for templates Protein Data Bank (PDB) entries 1CXP [16 (link)], 1EMO [29 (link)], and 1VVD [30 (link)], respectively. Specifically, we used the following residues for modelling: MPO-like domain (residues 142–738 modelled using residues 167–744 from template 1CXP, 47% sequence identity), CCP-like domain (residues 740–795 modelled using residues 147–202 from template 1VVD, 35% sequence identity), and EGF-like domain (residues 798–839 modelled using residues 2162–2205 from template 1EMO, 39% sequence identity). The cholinesterase-like (ChEL) domain of thyroglobulin was modelled using the crystal structure of recombinant human acetylcholinesterase in the apo state (PDB ID: 4EY4) [31 (link)] as a template. Transmembrane regions of TPO were identified using the membrane protein prediction server TMHMM [32 (link)], which found a transmembrane helix immediately after the EGF-like domain. A putative helix-helix interaction motif was identified as reported [33 (link)]. For the generation of the transmembrane helices dimer, the structure of a GxxxG motif dimer (PDB ID: 2L2T)[34 (link)] was used as a template. 200 homology models of human TPO (residues 142–880) were built using MODELLER v9.12 [35 (link)] and sorted by their Discrete Optimized Protein Energy (DOPE) score. The inter-dimer disulfide bridge (residues 153 in 1CXP) was modelled in the TPO dimer model, as was the iron-protoporphyrin IX (heme) group. Symmetry was maintained using MODELLER symmetry restraints between the two chains. Model plausibility was assessed by visual inspection of domain juxtaposition, and by determining the quality of the models using three separate assessments of model quality: (1) VERIFY 3D [36 (link)], which determines the compatibility of an atomic model with its own amino acid sequence by assigning a structural class based on its location and environment (alpha, beta, loop, polar, nonpolar etc.) and comparing the results to good structures. All models pass the VERIFY 3D test; (2) MolProbity [37 (link)], a widely used method (used by the PDB, for example) to asses the stereochemical quality of structures; (3) QMEAN Server for model quality estimation [38 (link)] (http://swissmodel.expasy.org/qmean), a method for the estimation of the absolute quality of individual protein structure models which is independent of protein size.
Le S.N., Porebski B.T., McCoey J., Fodor J., Riley B., Godlewska M., Góra M., Czarnocka B., Banga J.P., Hoke D.E., Kass I, & Buckle A.M. (2015). Modelling of Thyroid Peroxidase Reveals Insights into Its Enzyme Function and Autoantigenicity. PLoS ONE, 10(12), e0142615.
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Publication 2015
Acetylcholinesterase Amino Acid Sequence Butyrylcholinesterase Disulfides Equus asinus Helix (Snails) Heme Homo sapiens iron protoporphyrin IX Membrane Proteins Proteins Staphylococcal Protein A Thyroglobulin
5
Cholinesterase Inhibitory Activity Assay
Cited 4 times
ChE inhibitory activity was measured using Ellman’s method, as reported previously32
,33 (link). Sample solution aliquot (50 µL, 2 mg/mL) was mixed with 125 µL 5,5-dithio-bis(2-nitrobenzoic) acid (DTNB) and acetylcholinesterase (AChE from Electric eel, Type-VI-S, EC 3.1.1.7, Sigma, Saint Louis, MO), or butyrylcholinesterase (BChE from horse serum, EC 3.1.1.8, Sigma, Saint Louis, MO) solution (25 µL) in Tris-HCl buffer (pH 8.0) in a 96-well microplate and incubated for 15 min at 25 °C. The reaction was then initiated with the addition of acetylthiocholine iodide (ATCI) or butyrylthiocholine chloride (BTCl) (25 µL). Similarly, a blank was prepared by adding sample solution to all reaction reagents without enzyme(s) (AChE or BChE) solution. The sample and blank absorbances were recorded at 405 nm after 10 min incubation at 25 °C. The absorbance of the blank was subtracted from that of the sample and the cholinesterase inhibitory activity was expressed as milligrams of galanthamine equivalents (mg GALAE/g extract).
Mocan A., Zengin G., Simirgiotis M., Schafberg M., Mollica A., Vodnar D.C., Crişan G, & Rohn S. (2017). Functional constituents of wild and cultivated Goji (L. barbarum L.) leaves: phytochemical characterization, biological profile, and computational studies. Journal of Enzyme Inhibition and Medicinal Chemistry, 32(1), 153-168.
Publication 2017
Acetylcholinesterase acetylthiocholine iodide Butyrylcholinesterase Butyrylthiocholine Chlorides Cholinesterases Dithionitrobenzoic Acid Electric Eel Enzymes Equus caballus Galantamine Nitrobenzoic Acids Pain Psychological Inhibition Serum Tromethamine

Most recents protocols related to «Butyrylcholinesterase»

1
Localization of Tibialis Anterior Motor Points
The endplates in the TA muscle are not sharply demarcated and are distributed along the whole muscle by staining longitudinal cryosections for cholinesterase (7 (link)). Despite the staining motor point demarcation, other descriptions, using an electrophysiological analysis, found the main motor point located at the proximal third of the TA muscle belly (8 (link)). Botter et al. (9 (link)) found another minor motor point located distally and laterally between the middle and the distal third. The main motor point could be localized by Buchthal et al. (1 (link)) tracing a line between the tibial bone tuberosity at the knee down to a median line between the two malleoli; the limit between the upper and the middle third is the reference point and (2 (link)) tracing a line between the fibular head and the medial malleolus; the limit between the upper and the middle third is the reference point (10 (link)).
Kouyoumdjian J.A, & Graca C.R. (2023). Muscle fiber conduction velocity in situ revisited: A new approach to an ancient technique. Frontiers in Neurology, 14, 1118510.
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Publication 2023
Bones Butyrylcholinesterase Cryoultramicrotomy Fibula Head Knee Joint Muscle Tissue Tibia
2
Comprehensive Physiological Monitoring in Exercise Response
Before HTT, an initial blood sample was collected using an EDTA.K2 anticoagulant tube. A total of 8 ml of venous blood was taken from the patients’ cubital vein. The initial physiological indicators (SBP, DBP, HR, SaO2, and Tcore) were also measured. After HTT, post-exercise blood samples were collected immediately, and physiological data were measured after 5-min breaking. Twenty-four hours after HTT, blood samples for the recovery period were gathered. The feces were collected in the morning of two HTTs as pre-training and post-training samples. Clean cotton swabs were used to collect fresh fecal samples (5–10 g, no mix of urine, disinfectant, and sewage) into 15 ml sterile test tubes. Furthermore, the contents of organ injury biomarkers in plasma were detected, including alanine aminotransferase (ALT), alkaline phosphatase (AST), alkaline phosphatase (ALP), bilirubin, lactic dehydrogenase (LDH), alpha-hydroxybutyric dehydrogenase (α-HBDH), creatinine, urea nitrogen, cholinesterase, creatine kinase, prothrombin time (PT), activated partial prothrombin time (APTT), international normalized ratio (INR), Na+, K+, white blood cell (WBC), platelet (PLT), and hemoglobin.
Liu S., Wen D., Feng C., Yu C., Gu Z., Wang L., Zhang Z., Li W., Wu S., Liu Y., Duan C., Zhuang R, & Xue L. (2023). Alteration of gut microbiota after heat acclimation may reduce organ damage by regulating immune factors during heat stress. Frontiers in Microbiology, 14, 1114233.
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Publication 2023
Activated Partial Thromboplastin Time Alkaline Phosphatase Anticoagulants Bilirubin Biological Markers BLOOD Blood Platelets Butyrylcholinesterase Creatine Kinase Creatinine D-Alanine Transaminase Edetic Acid Feces Gossypium Hemoglobin Injuries International Normalized Ratio Leukocytes Nitrogen Oxidoreductase Patients physiology Plasma Sewage Sterility, Reproductive Times, Prothrombin Urea Urine Veins
3
Cholinesterase Enzyme Assay Protocol
Acetylcholinesterase from electric eel type VI-S, butyrylcholinesterase from equine serum, acetylthiocholine iodide (ATCI), butyrylthiocholine iodide (BTCI), 5,5′-dithiobis[2-nitrobenzoic acid] (DTNB), bovine serum albumin (BSA), tris buffer, and galantamine were purchased from Sigma–Aldrich. The organic solvents (methanol and ethanol) and reagents used in the analysis were of analytical grades.
S.u.c.i.a.t.i., Laili E.R., Ekasari W., K.u.a.t.m.a.n., Nuengchamnong N, & Suphrom N. (2023). Chemical Profiles and In Vitro Cholinesterase Inhibitory Activities of the Flower Extracts of Cassia spectabilis. Advances in Pharmacological and Pharmaceutical Sciences, 2023, 6066601.
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Publication 2023
Acetylcholinesterase acetylthiocholine iodide Butyrylcholinesterase Butyrylthiocholine Dithionitrobenzoic Acid Electric Eel Equus caballus Ethanol Galantamine Iodides Methanol Nitrobenzoic Acids Serum Serum Albumin, Bovine Solvents Tromethamine
4
Cholinesterase Activity Assay
Acetylcholine iodide, butyrylcholine
iodide, 5,5-dithio-bis-nitrobenzoic acid (DTNB), electric eel acetylcholinesterase
(type-VI-S), equine butyrylcholinesterase, 2,2-diphenyl-1-picrylhydrazyl
(DPPH), 2,2′-azinobis-3-ethylbenzothiazoline-6-sulfonic acid
(ABTS), HPLC-grade methanol, donepezil, and scopolamine were purchased
from Sigma-Aldrich. All chemicals and solvents used were of analytical
grades.
Karim N., Khan I., Khan I., Halim S.A., Khalid A., Abdalla A.N., Rehman N.U., Khan A, & Al-Harrasi A. (2023). Antiamnesic Effects of Novel Phthalimide Derivatives in Scopolamine-Induced Memory Impairment in Mice: A Useful Therapy for Alzheimer’s Disease. ACS Omega, 8(8), 8052-8065.
Publication 2023
2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid Acetylcholine Iodide Acetylcholinesterase Butyrylcholinesterase diphenyl Donepezil Electric Eel Equus caballus High-Performance Liquid Chromatographies Methanol Nitrobenzoic Acids Scopolamine Solvents Sulfonic Acids
5
Cholinesterase Inhibition Assay for AChE and BChE
The inhibitory activity of 1–3 for AChE and BChE was determined spectrophotometrically using modified Ellman’s method [25 (link)] to quantify them in terms of IC50 values.
The enzyme activity in the final reaction mixture (2000 µL) was 0.2 U/mL, the concentration of ATCh (or BTCh) was 40 µM, and the concentration of DTNB was 100 µM for all reactions. The investigated derivatives were dissolved in DMSO and then diluted with demineralized water (conductivity 3 μS, equipment supplier BKG Water Treatment, Hradec Králové, Czech Republic) to a concentration of 1000 µM. Five different inhibitor concentrations were used for all tested compounds in the final reaction mixture. The final concentration of DMSO was 0.2%. All experiments were performed in triplicate. The average values of the reaction rate (v0-uninhibited reaction, vi-inhibited reaction) were used to construct the dependence of v0/vi on the concentration of inhibitors. IC50 values were calculated from obtained regression curve equations.
Acetylcholinesterase originating from electric eels (Electrophorus electricus L.; EeAChE) and butyrylcholinesterase obtained from equine serum (EqBChE) were used. The clinically used drug rivastigmine was involved as a reference dual AChE and BChE inhibitor. All enzymes, substrates and rivastigmine were purchased from Merck (Prague, Czech Republic).
Houngbedji N.H., Štěpánková Š., Pflégr V., Svrčková K., Švarcová M., Vinšová J, & Krátký M. (2023). Novel Inhibitors of Acetyl- and Butyrylcholinesterase Derived from Benzohydrazides: Synthesis, Evaluation and Docking Study. Pharmaceuticals, 16(2), 172.
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Publication 2023
Acetylcholinesterase Butyrylcholinesterase derivatives Dithionitrobenzoic Acid Electric Conductivity Electric Eel enzyme activity Enzymes Equus caballus inhibitors Pain Pharmaceutical Preparations Psychological Inhibition Rivastigmine Serum Sulfoxide, Dimethyl

Top products related to «Butyrylcholinesterase»

1
Acetylthiocholine iodide by Merck Group
Sourced in United States, Germany, United Kingdom, Spain, Italy, China, Sao Tome and Principe, Canada, India, Thailand, Japan, Switzerland, France, Argentina, Portugal
Acetylthiocholine iodide is a chemical compound used as a substrate in enzymatic assays. It is commonly employed in the measurement of the activity of the enzyme acetylcholinesterase.
2
Acetylcholinesterase by Merck Group
Sourced in United States, Germany, Italy, Chile, Spain
Acetylcholinesterase is an enzyme that catalyzes the breakdown of the neurotransmitter acetylcholine in the synaptic cleft. It is an important component in the regulation of nerve impulse transmission.
3
Butyrylcholinesterase by Merck Group
Sourced in Germany, United States, Italy
Butyrylcholinesterase is an enzyme that catalyzes the hydrolysis of the neurotransmitter acetylcholine. It is found in various tissues and plays a role in the regulation of cholinergic neurotransmission.
4
Butyrylthiocholine iodide by Merck Group
Sourced in United States, Germany, United Kingdom, Italy
Butyrylthiocholine iodide is a chemical compound used in various laboratory applications. It functions as a substrate for the enzyme butyrylcholinesterase, which is commonly used in the analysis and detection of this enzyme.
5
Gallic acid by Merck Group
Sourced in United States, Germany, Italy, Spain, France, India, China, Poland, Australia, United Kingdom, Sao Tome and Principe, Brazil, Chile, Ireland, Canada, Singapore, Switzerland, Malaysia, Portugal, Mexico, Hungary, New Zealand, Belgium, Czechia, Macao, Hong Kong, Sweden, Argentina, Cameroon, Japan, Slovakia, Serbia
Gallic acid is a naturally occurring organic compound that can be used as a laboratory reagent. It is a white to light tan crystalline solid with the chemical formula C6H2(OH)3COOH. Gallic acid is commonly used in various analytical and research applications.
6
5 5 dithiobis 2 nitrobenzoic acid by Merck Group
Sourced in United States, Germany, India, China, Italy, United Kingdom, Japan, Spain, Israel, Canada, Argentina
5,5′-dithiobis(2-nitrobenzoic acid) is a chemical compound used in various laboratory applications. It is a solid, crystalline substance with a specific chemical structure and formula. The primary function of this compound is to serve as a reagent in analytical and biochemical procedures, without further interpretation of its intended use.
7
5 5 dithiobis 2 nitrobenzoic acid dtnb by Merck Group
Sourced in United States, Germany, China, Italy, India, Switzerland, Spain, United Kingdom, Sao Tome and Principe
5,5′-dithiobis(2-nitrobenzoic acid) (DTNB) is a chemical compound used in various laboratory applications. It is a water-soluble, yellow-colored reagent that is commonly employed for the determination of thiol groups in proteins and other biological samples.
8
Quercetin by Merck Group
Sourced in United States, Germany, Italy, India, Spain, United Kingdom, France, Poland, China, Sao Tome and Principe, Australia, Brazil, Macao, Switzerland, Canada, Chile, Japan, Singapore, Ireland, Mexico, Portugal, Sweden, Malaysia, Hungary
Quercetin is a natural compound found in various plants, including fruits and vegetables. It is a type of flavonoid with antioxidant properties. Quercetin is often used as a reference standard in analytical procedures and research applications.
9
2 2 diphenyl 1 picrylhydrazyl (dpph) by Merck Group
Sourced in United States, Germany, Italy, India, China, Spain, Poland, France, United Kingdom, Australia, Brazil, Singapore, Switzerland, Hungary, Mexico, Japan, Denmark, Sao Tome and Principe, Chile, Malaysia, Argentina, Belgium, Cameroon, Canada, Ireland, Portugal, Israel, Romania, Czechia, Macao, Indonesia
DPPH is a chemical compound used as a free radical scavenger in various analytical techniques. It is commonly used to assess the antioxidant activity of substances. The core function of DPPH is to serve as a stable free radical that can be reduced, resulting in a color change that can be measured spectrophotometrically.
10
Formic acid by Merck Group
Sourced in Germany, United States, Italy, United Kingdom, France, Spain, China, Poland, India, Switzerland, Sao Tome and Principe, Belgium, Australia, Canada, Ireland, Macao, Hungary, Czechia, Netherlands, Portugal, Brazil, Singapore, Austria, Mexico, Chile, Sweden, Bulgaria, Denmark, Malaysia, Norway, New Zealand, Japan, Romania, Finland, Indonesia
Formic acid is a colorless, pungent-smelling liquid chemical compound. It is the simplest carboxylic acid, with the chemical formula HCOOH. Formic acid is widely used in various industrial and laboratory applications.

More about "Butyrylcholinesterase"

Butyrylcholinesterase (BChE), also known as pseudocholinesterase, is an enzyme that plays a crucial role in the metabolism and regulation of certain drugs and compounds.
It is primarily found in the liver, pancreas, and plasma, and is responsible for the hydrolysis of butyrylcholine and other choline esters.
BChE is closely related to its counterpart, Acetylcholinesterase (AChE), which is involved in the breakdown of the neurotransmitter acetylcholine.
While AChE is primarily found in the nervous system and muscle tissues, BChE has a more diverse distribution and function.
One of the key roles of BChE is its protective function against organophosphate poisoning.
Organophosphates are a class of compounds that can inhibit cholinesterase enzymes, leading to the accumulation of acetylcholine and potentially life-threatening effects.
BChE can act as a 'scavenger,' binding to and inactivating these harmful compounds, thereby reducing their toxicity.
In addition to its role in drug metabolism, BChE has been studied for its potential therapeutic applications.
Researchers have explored the use of BChE as a treatment for conditions such as Alzheimer's disease, where the enzyme may help to regulate the levels of acetylcholine in the brain.
BChE has also been investigated for its ability to metabolize certain drugs, which could have implications for personalized medicine and dosage optimization.
To study BChE and its functions, researchers often utilize various substrates and reagents, such as butyrylthiocholine iodide, acetylthiocholine iodide, and DTNB (5,5'-dithiobis(2-nitrobenzoic acid)).
These compounds can be used to measure BChE activity and assess its interactions with other molecules.
Overall, the study of Butyrylcholinesterase provides valuable insights into its biological functions and potential therapeutic applications, with implications for drug development, toxicology, and personalized medicine.
By understanding the role of BChE in the body, researchers can further explore its clinical relevance and develop new strategies for addressing a range of health conditions.