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Thematische Bibliographien / Butyrylcholinesterase activity / Zeitschriftenartikel

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Zeitschriftenartikel zum Thema „Butyrylcholinesterase activity“

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Veröffentlicht am 18. Mai 2024

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1

Goliasch, Georg, Arvand Haschemi, Rodrig Marculescu, Georg Endler, Gerald Maurer, Oswald Wagner, Kurt Huber, Christine Mannhalter und Alexander Niessner. „Butyrylcholinesterase Activity Predicts Long-Term Survival in Patients with Coronary Artery Disease“. Clinical Chemistry 58, Nr. 6 (01.06.2012): 1055–58. http://dx.doi.org/10.1373/clinchem.2011.175984.

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Abstract BACKGROUND Low serum butyrylcholinesterase activity was associated with all-cause and cardiovascular mortality in a community-based study; however, there are no data from investigations of the long-term effects of butyrylcholinesterase on mortality in patients with diagnosed coronary artery disease (CAD). We therefore assessed the effect of butyrylcholinesterase activity on the outcomes of patients with CAD. METHODS AND RESULTS We prospectively included 720 patients in our study: 293 patients with stable CAD and 427 patients with acute coronary syndrome. During a median follow-up of 11.3 years corresponding to 6469 overall person-years, 278 deaths (38.6%) were recorded. We detected a significant and independent protective effect of butyrylcholinesterase on all-cause mortality [adjusted hazard ratio (HR) for a 1-SD increase, 0.62; 95% CI, 0.54–0.71; P < 0.001] and cardiovascular mortality (adjusted HR, 0.64; 95% CI, 0.54–0.76; P < 0.001) in a Cox proportional hazards regression analysis. The 10-year survival rates were 42%, 74%, and 87% in the first, second, and third tertiles of butyrylcholinesterase activity. The presentation of CAD affected the effect of butyrylcholinesterase on mortality (P for interaction = 0.012), with a stronger association found in patients with stable CAD (adjusted HR, 0.56; 95% CI, 0.45–0.70; P < 0.001). CONCLUSIONS Our study demonstrates a strong inverse association between butyrylcholinesterase activity and long-term outcome in patients with known CAD. Because butyrylcholinesterase added predictive information after adjustment for established cardiovascular risk factors, additional underlying pathophysiological mechanisms and the potential applicability of butyrylcholinesterase activity for secondary risk prediction needs to be addressed in future studies.

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Abbott, C. A., M. I. MacKness, S. Kumar, A. O. Olukoga, C. Gordon, S. Arrol, D. Bhatnagar, A. J. M. Boulton und P. N. Durrington. „Relationship between Serum Butyrylcholinesterase Activity, Hypertriglyceridaemia and Insulin Sensitivity in Diabetes Mellitus“. Clinical Science 85, Nr. 1 (01.07.1993): 77–81. http://dx.doi.org/10.1042/cs0850077.

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1. The activity of serum butyrylcholinesterase (‘pseudocholinesterase’, EC3.1.1.8) was investigated in 56 patients with type 1 diabetes mellitus, 51 patients with type 2 diabetes mellitus and 101 healthy control subjects. 2. Butyrylcholinesterase activity was significantly elevated in both type 1 (8.10 ± 3.35 units/ml) and type 2 (7.22 ± 1.95 units/ml) diabetes compared with the control subjects (4.23 ± 1.89 units/ml) (P <0.001). 3. In the patients with type 1 and type 2 diabetes, serum butyrylcholinesterase activity was correlated with log serum fasting triacylglycerol concentration (r = 0.41 and r = 0.43, respectively, P <0.001). In the type 2 population serum butyrylcholinesterase activity was also correlated with insulin sensitivity (r = −0.51, P <0.001). 4. Serum butyrylcholinesterase activity was unrelated to age, gender, serum γ-glutamyltranspeptidase activity, body mass index, or treatment for diabetes in both the diabetic populations. 5. In 37 non-diabetic patients with butyrylcholinesterase deficiency serum triacylglycerol levels were in the normal range. 6. These results are consistent with the view that butyrylcholinesterase may have a role in the altered lipoprotein metabolism in hypertriglyceridaemia associated with insulin insensitivity or insulin deficiency in diabetes mellitus.

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Mabrouk, Hajer, Haithem Mechria, Anouar Mechri, Houda Rahali, Wahiba Douki, Lotfi Gaha und Mohamed Fadhel Najjar. „Butyrylcholinesterase activity in schizophrenic patients“. Annales de biologie clinique 69, Nr. 6 (November 2011): 647–52. http://dx.doi.org/10.1684/abc.2011.0634.

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4

Suneetha, Lavanya M., Venkata Karunakar, Raj Gopal Reddy und Sujai Suneetha. „Serum Butyrylcholinesterase Activity in Leprosy“. International Journal of Leprosy and Other Mycobacterial Diseases 72, Nr. 3 (2004): 324. http://dx.doi.org/10.1489/0020-7349(2004)72<324:sbail>2.0.co;2.

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5

Kálmán, János, Anna Juhász, Zoltán Rakonczay, György Ábrahám, Krisztina Boda, Tibor Farkas, Botond Penke und Zoltán Janka. „Serum butyrylcholinesterase activity in hyperlipidaemia“. Atherosclerosis 173, Nr. 1 (März 2004): 145–46. http://dx.doi.org/10.1016/j.atherosclerosis.2003.12.002.

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Van Lith, H. A., und A. C. Beynen. „Dietary cholesterol lowers the activity of butyrylcholinesterase (EC3.1.1.8), but elevates that of esterase-1 (EC3.1.1.1) in plasma of rats“. British Journal of Nutrition 70, Nr. 3 (November 1993): 721–26. http://dx.doi.org/10.1079/bjn19930167.

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The question addressed is whether an increased intake of cholesterol affects esterase-1 (EC3.1.1.1; ES-1) and butyrylcholinesterase (EC3.1.1.8) activity in plasma. Rats were fed on a purified diet either without or with cholesterol (10 g/kg) added at the expense of the carbohydrate source. Dietary cholesterol significantly decreased plasma butyrylcholinesterase activity, but raised plasma ES-1 activity. Evidence is discussed, suggesting that plasma butyrylcholinesterase is involved in plasma cholesterol metabolism, whereas esterase-1 is involved in intestinal cholesterol absorption.

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Darvesh, Sultan, Andrea M. LeBlanc, Ian R. Macdonald, George A. Reid, Virender Bhan, Robert J. Macaulay und John D. Fisk. „Butyrylcholinesterase activity in multiple sclerosis neuropathology“. Chemico-Biological Interactions 187, Nr. 1-3 (September 2010): 425–31. http://dx.doi.org/10.1016/j.cbi.2010.01.037.

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8

Kuhl, David E., Robert A. Koeppe, Scott E. Snyder, Satoshi Minoshima, Kirk A. Frey und Michael R. Kilbourn. „Imaging butyrylcholinesterase activity in Alzheimer's disease“. Annals of Neurology 60, Nr. 6 (Dezember 2006): 746. http://dx.doi.org/10.1002/ana.21023.

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9

Vahdati-Mashhadian, Nasser, Mohammad K. Hassanzadeh, Javad Hosseini und Ali A. Saffareshargh. „Ethnic differences in the frequency of distribution of serum cholinesterase activity in the Iranian population“. Canadian Journal of Physiology and Pharmacology 82, Nr. 5 (01.05.2004): 326–30. http://dx.doi.org/10.1139/y04-030.

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One thousand Iranians belonging to 5 different Iranian ethnic groups were tested for butyrylcholinesterase (BChE) activity and phenotype. The phenotype was measured as percent inhibition in the presence of dibucaine. It was found that the Iranian population had an extraordinarily high frequency of the atypical variant of butyrylcholinesterase. 70% to 80% of Iranians carried the atypical mutation (Asp70Gly) on one allele. This contrasts with European and American populations where only 4% carry the atypical allele. The atypical variant of butyrylcholinesterase is known to be associated with prolonged apnea after administration of the muscle relaxants succinylcholine and mivacurium, and is also thought to be associated with abnormal sensitivity to cocaine toxicity. This study demonstrates that the ethnic background of a person has an important role in a person's response to drugs.Key words: butyrylcholinesterase, dibucaine number, heterozygous genes, different Iranian ethnics, metabolic polymorphism.

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Kulesh, A. A., und V. V. Schestakov. „MELATONIN SECRETION AND SERUM BUTYRYLCHOLINESTERASE ACTIVITY AS A POTENTIAL BIOMARKERS OF COGNITIVE IMPAIRMENT IN ACUTE ISCHEMIC STROKE“. National Journal of Neurology 2, Nr. 02 (30.11.2012): 66–70. http://dx.doi.org/10.61788/njn.v2i12.08.

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The assessment of melatonin secretion in 25 men and serum butyrylcholinesterase level in 40 patients was performed in acute period of stroke. The interaction between these parameters and cognitive state was analyzed. The low levels of 6-sulfatoxymelatonin in daily urine and butyrylcholinesterase in blood were revealed. The 6-sulfatoxymelatonin level in daily urine < 4,0 ng/ml can be regarded as a potential biological marker of poststoke memory dysfunction. The serum butyrylcholinesterase level < 7,0 nmol/sec-l can be regarded as a potential biochemical marker of the multifunctional type of poststoke cognitive impairment.

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Schumacher, Ilana, Aya Arad und Rimona Margalit. „Butyrylcholinesterase formulated in liposomes“. Biotechnology and Applied Biochemistry 30, Nr. 3 (Dezember 1999): 225–30. http://dx.doi.org/10.1111/j.1470-8744.1999.tb00774.x.

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Exogenous cholinesterases have the potential to take part in defence against organophosphate toxins, by acting as scavenger systems. Postulating that formulation in liposomes could enhance the toxin‐scavenging potential of these enzymes, we have initiated studies of such formulations and are reporting here our first steps, exploring butyrylcholinesterase (BChE) in multilamellar liposomes composed of phosphatidylcholine. We started by developing an essential research tool: a multisample, sensitive and rapid enzyme‐activity assay, based on the Ellman reaction, that could be performed directly on liposome‐containing samples. Using an ELISA reader equipped to follow time‐dependant absorbency changes, 10 min sufficed to assay 96 samples simultaneously. Next, several key properties of liposome‐formulated BChE were explored and the major findings were: (i) the encapsulated enzyme was found to retain its activity. (ii) Enzyme activity was found to increase (at constant enzyme concentration) in the presence of the lipid, in a lipid‐concentration‐dependant manner. Through data analysis it was possible to attribute this effect to changes in k cat. (iii) Good, reproducible, encapsulation efficiencies (for macromolecules) in the range of 30% were obtained at liposome concentrations of 100 mM lipid. (iv) Free BChE was completely susceptible to proteolysis under conditions mimicking enzymically‐hostile biological environments, whereas 60% of the liposome‐formulated BChE was protected, found to be inaccessible to the proteolytic enzymes. (v) Short‐term exposures of free and liposome‐encapsulated BChE to the inhibitor paraoxon, generated significant losses in enzyme activity. Residual activities of both BChE formulations dropped considerably over the paraoxon concentration range of 0.02–0.11 μM, down to 3 and 11% for free and liposome‐encapsulated enzyme respectively. These data are a clear indication that the encapsulated BChE was accessible to the inhibitor, indicating that such liposomal formulations have the potential to perform as the desired scavenger systems.

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Mangas, Iris, Eugenio Vilanova und Jorge Estévez. „Phenyl valerate esterase activity of human butyrylcholinesterase“. Archives of Toxicology 91, Nr. 10 (15.03.2017): 3295–305. http://dx.doi.org/10.1007/s00204-017-1946-5.

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13

Müller, Tatiane C., João Batista T. Rocha, Vera M. Morsch, Roseli Tatto Neis und Maria R. C. Schetinger. „Antidepressants inhibit human acetylcholinesterase and butyrylcholinesterase activity“. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1587, Nr. 1 (Mai 2002): 92–98. http://dx.doi.org/10.1016/s0925-4439(02)00071-6.

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Ullah, Himayat, Khair Zaman und Muhammad Ismail. „Microwave Assisted Synthesis of BenzilideneBenzylamine and Its Acetylcholinesterase and Butyrylcholinesterase Activity“. Journal of Tropical Pharmacy and Chemistry 5, Nr. 2 (23.07.2020): 86–94. http://dx.doi.org/10.25026/jtpc.v5i2.236.

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BenzilideneBenzylamine the derivative of Schiff bases contain azomethine group already used widely for industrial purposes and have wide range of biological activities. Benzilidene Benzylamine were synthesized by microwave irradiation reacting different aromatic and aniline purified pure crystal, 85% yield obtained reaction monitor by TLC. The Anticholinesterase activity utilized spectrophotometric Ellman assay for determination of butyrylcholinesterase and acetylcholinesterase. The synthesis compound 1 – 6 showed a wide range of inhibitory activity the compound 3((E)-N-(4-fluorobenzylidene)aniline) at 1000µg/mL, 71.62±0.74 percent inhibitory acetylcholinesterase potential while compound 6 ((E)-4 ((phenylimino)methyl) benzaldehyde) at 500 and 1000 µg/mL at IC50 show 71.68±0.22, 77.84±0.32 percent inhibitory potential comparatively greater than standard Galanthamine at 62.5µg/mL, 74.10±0.90 at IC50. The butyrylcholinesterase activity of compound 6 ((E)-4 ((phenylimino)methyl)benzaldehyde) at 1000 µg/mL, show 75.83±1.07 percent inhibitory potential which is similar to standard compound at 62.5µg/mL concentration of 75.45±0.90 percent butyrylcholinesterase inhibitory activity.

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Levano, Soledad, Hans Ginz, Martin Siegemund, Miodrag Filipovic, Evgueni Voronkov, Albert Urwyler und Thierry Girard. „Genotyping the Butyrylcholinesterase in Patients with Prolonged Neuromuscular Block after Succinylcholine“. Anesthesiology 102, Nr. 3 (01.03.2005): 531–35. http://dx.doi.org/10.1097/00000542-200503000-00009.

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Background Succinylcholine remains the standard neuromuscular blocking drug for tracheal intubation in emergency situations. The short duration of action is due to its rapid hydrolytic degradation by butyrylcholinesterase (plasmacholinesterase). Multiple variants of this enzyme are known (A, F, S, H, J, K variants) with different effects on enzyme activity. This study was undertaken to evaluate the use of molecular genetic methods in patients with clinically prolonged neuromuscular block. Methods Nine patients with a neuromuscular block of 14 min to 5 h were selected. All four exons of the butyrylcholinesterase were amplified by polymerase chain reaction and analyzed by automated sequencing. Molecular genetic results were compared with clinical relaxation time and with biochemical test results (total butyrylcholinesterase activity, dibucaine and fluoride inhibition). Results Seven of nine patients were mutation carriers. Five of these had more than one mutation. The A and K variants were the most frequent variations. Three of four patients who were homozygous for the A variant were also carriers of the K allele. The authors identified one novel mutation (G1294T) introducing a stop codon at amino acid position 432. The duration of neuromuscular block was substantially different between patients with identical butyrylcholinesterase genotypes. Conclusions Variations in the genetic sequence of butyrylcholinesterase are frequent in patients with prolonged duration of action of succinylcholine. Direct sequencing of the whole butyrylcholinesterase gene is an appropriate method for genotyping and, accordingly, should be used in future clinical studies with drugs metabolized by this enzyme (e.g., succinylcholine, mivacurium).

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Panhuizen, Ivo F., Marc M. J. Snoeck, Soledad Levano und Thierry Girard. „Prolonged Neuromuscular Blockade Following Succinylcholine Administration to a Patient with a Reduced Butyrylcholinesterase Activity“. Case Reports in Medicine 2010 (2010): 1–4. http://dx.doi.org/10.1155/2010/472389.

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This case is about a 48-year-old woman known with a reduced butyrylcholinesterase activity, who developed prolonged neuromuscular blockade following the unintentional administration of succinylcholine. We took the opportunity to monitor the development of neuromuscular function during this period and blood samples were taken for molecular genetic analysis and for quantitative and qualitative analysis since not all causative mutations are functionally characterized. Reduced butyrylcholinesterase activity is discussed in many aspects. Clinical considerations are suggested concerning genetic counselling.

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Kolesnikov, Ilya, Anastasia Khokhlova, Dmitry Pankin, Anna Pilip, Anastasia Egorova, Vladislav Zigel, Maxim Gureev, Gerd Leuchs und Alina Manshina. „Laser-induced switching of the biological activity of phosphonate molecules“. New Journal of Chemistry 45, Nr. 34 (2021): 15195–99. http://dx.doi.org/10.1039/d1nj02487f.

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Zivkovic, Aleksandar R., Karsten Schmidt, Annette Sigl, Sebastian O. Decker, Thorsten Brenner und Stefan Hofer. „Reduced Serum Butyrylcholinesterase Activity Indicates Severe Systemic Inflammation in Critically Ill Patients“. Mediators of Inflammation 2015 (2015): 1–11. http://dx.doi.org/10.1155/2015/274607.

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Systemic inflammation is an immune response to a nonspecific insult of either infectious or noninfectious origin and remains a challenge in the intensive care units with high mortality rate. Cholinergic neurotransmission plays an important role in the regulation of the immune response during inflammation. We hypothesized that the activity of butyrylcholinesterase (BChE) might serve as a marker to identify and prognose systemic inflammation. By using a point-of-care-testing (POCT) approach we measured BChE activity in patients with severe systemic inflammation and healthy volunteers. We observed a decreased BChE activity in patients with systemic inflammation, as compared to that of healthy individuals. Furthermore, BChE activity showed an inverse correlation with the severity of the disease. Although hepatic function has previously been found essential for BChE production, we show here that the reduced BChE activity associated with systemic inflammation occurs independently of and is thus not caused by any deficit in liver function in these patients. A POCT approach, used to assess butyrylcholinesterase activity, might further improve the therapy of the critically ill patients by minimizing time delays between the clinical assessment and treatment of the inflammatory process. Hence, assessing butyrylcholinesterase activity might help in early detection of inflammation.

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Ekerendu, Effiong E., Uchechukwu C. Okoro, Cosmas C. Eze, David S. Khanye, Kingsley O. Omeje, Narendra K. Mishra und David I. Ugwu. „Novel Cholinesterase Inhibitors: Synthesis, in silico and in vitro Studies“. Asian Journal of Chemistry 35, Nr. 7 (2023): 1683–91. http://dx.doi.org/10.14233/ajchem.2023.27588.

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The synthesis of new functionalized linear diaza and triaza phenothiazine and phenoxazines and their in silico and in vitro anti-Alzheimer activity is reported. Fifteen new amide derivatives (8-11 & 13-24) were synthesized by the reactions of phenothiazines/phenoxazine (6 or 12) and various aliphatic and aromatic primary amides (7) in the presence of nickel catalyst and anhydrous potassium carbonate under nitrogen atmosphere. The FTIR, 1H NMR, 13C NMR and HR-MS spectra of the synthesized compounds were in agreement with the assigned structures. All the 15 new derivatives were screened for their in silico and in vitro anti-Alzheimer’s activity using the inhibition of acetylcholinesterase and butyrylcholinesterase. The results of the in silico experiment showed that most of the synthesized derivatives had good binding energies, binding interaction and bond distances. The most active derivatives in the in silico studies was compounds 18 (-12.5 and -11.5 kcal/mol) against acetylcholinesterase and butyrylcholinesterase, respectively. In addition, compound 18 had the best in vitro inhibitory activity against acetylcholinesterase and butyrylcholinesterase (99.37% and 82.35%). The results of in silico experiment were greatly in agreement with the results of in vitro studies. The structure-activity relationship studies revealed that the phenothiazine derivatives had better in silico and in vitro activities. Furthermore, 2-substitutted phenothiazines had better activity than the unsubstituted phenothiazines. The synthesized compounds showed promising in silico and in vitro activities against acetylcholinesterase and butyrylcholinesterase and as such could be further developed for the treatment of Alzheimer’s disease.

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Adalat, Bushra, Fazal Rahim, Wajid Rehman, Zarshad Ali, Liaqat Rasheed, Yousaf Khan, Thoraya A. Farghaly et al. „Biologically Potent Benzimidazole-Based-Substituted Benzaldehyde Derivatives as Potent Inhibitors for Alzheimer’s Disease along with Molecular Docking Study“. Pharmaceuticals 16, Nr. 2 (30.01.2023): 208. http://dx.doi.org/10.3390/ph16020208.

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Twenty-one analogs were synthesized based on benzimidazole, incorporating a substituted benzaldehyde moiety (1–21). These were then screened for their acetylcholinesterase and butyrylcholinesterase inhibition profiles. All the derivatives except 13, 14, and 20 showed various inhibitory potentials, ranging from IC50 values of 0.050 ± 0.001 µM to 25.30 ± 0.40 µM against acetylcholinesterase, and 0.080 ± 0.001 µM to 25.80 ± 0.40 µM against butyrylcholinesterase, when compared with the standard drug donepezil (0.016 ± 0.12 µM and 0.30 ± 0.010 µM, against acetylcholinesterase and butyrylcholinesterase, respectively). Compound 3 in both cases was found to be the most potent compound due to the presence of chloro groups at the 3 and 4 positions of the phenyl ring. A structure-activity relationship study was performed for all the analogs except 13, 14, and 20, further, molecular dynamics simulations were performed for the top two compounds as well as the reference compound in a complex with acetylcholinesterase and butyrylcholinesterase. The molecular dynamics simulation analysis revealed that compound 3 formed the most stable complex with both acetylcholinesterase and butyrylcholinesterase, followed by compound 10. As compared to the standard inhibitor donepezil both compounds revealed greater stabilities and higher binding affinities for both acetylcholinesterase and butyrylcholinesterase.

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Araoud, Manel, Fadoua Neffeti, Wahiba Douki, Hassen Ben Hfaiedh, Mohamed Akrout, Mohamed Fadhel Najjar und Abderraouf Kenani. „Factors influencing plasma butyrylcholinesterase activity in agricultural workers“. Annales de biologie clinique 69, Nr. 2 (März 2011): 159–66. http://dx.doi.org/10.1684/abc.2011.0531.

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Montenegro, María F., María T. Moral-Naranjo, María Páez de la Cadena, Francisco J. Campoy, Encarnación Muñoz-Delgado und Cecilio J. Vidal. „Human butyrylcholinesterase components differ in aryl acylamidase activity“. Biological Chemistry 389, Nr. 4 (01.04.2008): 425–32. http://dx.doi.org/10.1515/bc.2008.041.

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Abstract Apart from its esterase activity, butyrylcholinesterase (BuChE) displays aryl acylamidase (AAA) activity able to hydrolyze o-nitroacetanilide (ONA) and its trifluoro-derivative (F-ONA). We report here that, despite amidase and esterase sites residing in the same protein, in human samples depleted of acetylcholinesterase the ratio of amidase to esterase activity varied depending on the source of BuChE. The much faster degradation of ONA and F-ONA by BuChE monomers (G1) of colon and kidney than by the tetramers (G4) suggests aggregation-driven differences in the AAA site between single and polymerized subunits. The similar ratio of F-ONA to butyrylthiocholine hydrolysis by serum G1 and G4 forms support structural differences in the amidase site according to the source of BuChE. The changing ratios of amidase to esterase activities in the human sources probably arise from post-translational modifications in BuChE subunits, the specific proportion of monomers and oligomers and the variable capacity of the tetramers for degrading ONA and F-ONA. The elevated amidase activity of BuChE monomers and the scant activity of the tetramers justify the occurrence of single BuChE subunits in cells as a means to sustain the AAA activity of BuChE which otherwise could be lost by tetramerization.

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Carmona, Gilberto N., Charles W. Schindler, Mohammed Shoaib, Rebecca Jufer, Edward J. Cone, Steven R. Goldberg, Nigel H. Greig, Qian-Sheng Yu und David A. Gorelick. „Attenuation of cocaine-induced locomotor activity by butyrylcholinesterase.“ Experimental and Clinical Psychopharmacology 6, Nr. 3 (1998): 274–79. http://dx.doi.org/10.1037/1064-1297.6.3.274.

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Tvarijonaviciute, A., J. J. Ceron und M. Caldin. „Serum butyrylcholinesterase activity in dogs with diabetes mellitus“. Veterinary Journal 192, Nr. 3 (Juni 2012): 494–97. http://dx.doi.org/10.1016/j.tvjl.2011.06.040.

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Domenech, Ivett Barreiro, Onel Fong Lores, Elio Cisnero Prego und Isolina Sanchez Jaca. „Michel electrometric modified method to determine Butyrylcholinesterase activity“. Toxicology Letters 172 (Oktober 2007): S207. http://dx.doi.org/10.1016/j.toxlet.2007.05.521.

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Gorelick, David A., John R. Cashman und Jennifer R. Schroeder. „Plasma butyrylcholinesterase enzyme functional activity in cocaine addicts“. Drug and Alcohol Dependence 146 (Januar 2015): e126. http://dx.doi.org/10.1016/j.drugalcdep.2014.09.261.

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Kuznetsova, L. P. „THE HORSE SERUM BUTYRYLCHOLINESTERASE ACTIVITY UNDER OCTANOL INFLUENCE“. Biotechnologia Acta 6, Nr. 6 (2013): 100–104. http://dx.doi.org/10.15407/biotech6.06.100.

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Cahlíková, Lucie, Nina Benešová, Kateřina Macáková, Radim Kučerac, Václav Hrstka, Jiří Klimeš, Luděk Jahodář und Lubomír Opletal. „Alkaloids from Some Amaryllidaceae Species and Their Cholinesterase Activity“. Natural Product Communications 7, Nr. 5 (Mai 2012): 1934578X1200700. http://dx.doi.org/10.1177/1934578x1200700506.

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Alkaloid extracts of four Amaryllidaceae species were studied with respect to their acetylcholinesterase and butyrylcholinesterase inhibitory activity and alkaloid patterns. Twenty-one alkaloids were determined by GC/MS, and seventeen of them identified from their mass spectra and retention times. The GC/MS analysis of the alkaloid extract of Nerine filamentosa is the first phytochemical investigation of this species. Promising erythrocytic acetylcholinesterase inhibitory activity was demonstrated by the alkaloid extracts of Narcissus poeticus var recurvus, Nerine filifolia and N. filamentosa (IC50,HuAChE = 6.0 ± 0.1 μg/mL; IC50,HuAChE = 18.5 ± 0.8 μg/mL, IC50,HuAChE = 21.6 ± 1.1 μg/mL). The most potent inhibitory activity against serum butyrylcholinesterase was shown by extracts of Sternbergia lutea and Nerine filamentosa (IC50,HuBuChE = 3.7 ± 0.1 μg/mL; IC50,HuBuChE = 13.0 ± 0.7 μg/mL).

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Snyder, Scott E., Neeraja Gunupudi, Phillip S. Sherman, Elizabeth R. Butch, Marc B. Skaddan, Michael R. Kilbourn, Robert A. Koeppe und David E. Kuhl. „Radiolabeled Cholinesterase Substrates: In Vitro Methods for Determining Structure-Activity Relationships and Identification of a Positron Emission Tomography Radiopharmaceutical for In Vivo Measurement of Butyrylcholinesterase Activity“. Journal of Cerebral Blood Flow & Metabolism 21, Nr. 2 (Februar 2001): 132–43. http://dx.doi.org/10.1097/00004647-200102000-00004.

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There is currently great interest in developing radiolabeled substrates for acetylcholinesterase and butyrylcholinesterase that would be useful in the in vivo imaging of patients with Alzheimer's disease. Using a simple in vitro spectrophotometric assay for determination of enzymatic cleavage rates, the structure-activity relationship for a short series of 1-methyl-4-piperidinyl esters was investigated. Relative enzymatic hydrolysis rates for the well-characterized 1-methyl-4-piperidinyl acetate, propionate, and i-butyrate esters were in agreement with literature values. The 4 and 5 carbon esters of 1-methyl-4-piperidinol were specific for butyrylcholinesterase and cleaved in the rank order n-valerate > n-butyrate >> 2-methylbutyrate, iso-valerate. These spectrophotometric results were also in agreement with in vitro hydrolysis rates in mouse blood and with in vivo regional retention of radioactivity in mouse brain of 11C-labeled analogs. Brain uptake and apparent enzymatic rate constants for 1-[11C]methyl-4-piperidinyl n-butyrate and n-valerate were calculated from in vivo measurements in M. nemistrina using positron emission tomography. Based on higher brain uptake of radioactivity and superior pharmacokinetics, 1-[11C]methyl-4-piperidinyl n-butyrate was identified as a new radiopharmaceutical for the in vivo measurement of butyrylcholinesterase activity.

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Saqib, Fatima, Khalid Hussain Janbaz und Maryam Khan Sherwani. „In vitro inhibitory potential of methanolic extract of Celosia argentea var. cristata on tyrosinase, acetylcholinesterase and butyrylcholinesterase enzymes“. Bangladesh Journal of Pharmacology 10, Nr. 2 (24.05.2015): 449. http://dx.doi.org/10.3329/bjp.v10i2.22880.

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<p>In the current study, methanol extract of <em>Celosia argentea</em> var. <em>cristata</em> was tested for its inhibitory potential against tyrosinase, acetylcholinesterase and butyrylcholinesterase enzymes at the concentration of 0.5 mM by ELISA microtiter plate assays. A significant tyrosinase inhibitory activity (63.6%), acetylcholinesterase inhibitory activity (80.3%) and butyrylcholinesterse inhibitory activity (68.24%) was shown by crude methanolic extract of <em>C. argentea</em> var. <em>cristata</em> with respective IC<sub>50 </sub>values of 268.5 ± 0.2 µg/mL, 73.6 ± 0.1 µg/mL and 132.8 ± 0.9 µg/mL. The result of this study reveals the use of <em>C. argentea</em> var. <em>cristata</em> in skin hyperpigmentation, Parkinson’s disease and neurodegenerative disorders like Alzheimer’s disease and dementia.</p>

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BHANUMATHY, C. D., und A. S. BALASUBRAMANIAN. „Evidence for a Zn2+-binding site in human serum butyrylcholinesterase“. Biochemical Journal 315, Nr. 1 (01.04.1996): 127–31. http://dx.doi.org/10.1042/bj3150127.

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Purified human serum butyrylcholinesterase after treatment with either of the metal chelators EDTA or NaCN was able to bind to a Zn2+-chelate–Sepharose affinity column and was eluted from the column by EDTA or imidazole. Prior EDTA treatment of the enzyme was essential for binding to this affinity column. The enzyme could be labelled with 65Zn2+ after EDTA treatment of the enzyme. Diethylpyrocarbonate modification of histidine residues in the EDTA-treated enzyme resulted in the abolition of both binding to the Zn2+-chelate–Sepharose column and labelling by 65Zn2+. Stoicheiometry of 65Zn2+ binding indicated approximately 0.85 mol of Zn2+/mol of subunit of the EDTA-treated enzyme. EDTA or NaCN treatment resulted in the loss of thermal stability of the enzyme at 37 °C which could not be reversed by Zn2+. Whereas the cholinesterase activity of butyrylcholinesterase was not affected by EDTA, there was significant loss of its carboxypeptidase activity in the presence of EDTA, and the loss could be reversed by added ZnCl2. These results suggest the presence of a Zn2+-binding site on human serum butyrylcholinesterase and the involvement of histidine residues in the metal binding. The presence in human serum butyrylcholinesterase of a sequence HXXE…H found in many known Zn2+-containing enzymes supports these findings.

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Shi, Da-Hua, Xiao-Dong Ma, Yu-Wei Liu, Wei Min, Fu-Jun Yin, Zong-Ming Tang, Meng-Qiu Song et al. „Synthesis, Crystal Structure and Biological Evaluation of Novel 2-Phenylthiazole Derivatives as Butyrylcholinesterase Inhibitors“. Journal of Chemical Research 42, Nr. 7 (Juli 2018): 366–70. http://dx.doi.org/10.3184/174751918x15314837408346.

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To find novel butyrylcholinesterase inhibitors, three novel 2-phenylthiazole derivatives were synthesised. The synthesised compounds were characterised by NMR and single-crystal X-ray diffraction analysis. Hirshfeld surface analysis and two-dimensional fingerprint plots of the compounds were used as a theoretical approach to assess the driving force for crystal structure formation via the intermolecular interactions in the crystal lattices of the synthesised compounds. Among the three compounds, N-(1,5-dimethyl-3-oxo-2-phenyl-2,3-dihydro- 1H-pyrazol-4-yl)-2-(4-methoxyphenyl)thiazole-4-carboxamide showed the best butyrylcholinesterase-inhibition activity with an IC50 value of 75.12 μM. A docking study demonstrated that this compound interacts with the peripheral anionic site of butyrylcholinesterase.

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Szwajgier, Dominik. „Anticholinesterase Activity of Phenolic Acids and their Derivatives“. Zeitschrift für Naturforschung C 68, Nr. 3-4 (01.04.2013): 125–32. http://dx.doi.org/10.1515/znc-2013-3-408.

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The ability of 36 phenolic acids and their derivatives to inhibit acetyl- and butyrylcholinesterase was studied. The most efficient acetylcholine inhibitors were: carnosic acid = gentisic acid > 3-hydroxy-4-methoxycinnamic acid = ethyl ferulate = ethyl vanillate = nordihydroguaiaretic acid > ethyl 4-hydroxybenzoate = methyl ferulate. The order of effectiveness towards butyrylcholinesterase was: carnosic acid > nordihydroguaiaretic acid = ethyl ferulate > salicylic acid > gentisic acid > rosmarinic acid = caftaric acid > homogentisic acid. The inhibitory activity was dependent on the number/position of OH or/and OCH3 groups attached to a phenol ring. It can be speculated that OCH3 substitution in the phenol ring can promote a higher antibutyrylcholinesterase activity (although not statistically confi rmed at p < 0.05). The presence of a CH=CH-COOH group had a highly favourable effect on the antiacetylcholinesterase activity compared with a CH2-CH2-COOH or a COOH group. Methyl and ethyl esters were more potent inhibitors than the corresponding free acids. The molecular weight of the compounds (in the range of M = 154.12 ~ 474 g/mol) played a minor role in this context.

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Бессарабов, В. І., Л. М. Вахітова, Г. І. Кузьміна, О. П. Баула, В. М. Лісовий und Н. П. Здерко. „РОЗРОБКА МЕТОДУ ОЦІНКИ ЕФЕКТИВНОСТІ ДЕКОНТАМІНАЦІЇ ФОСФОРОРГАНІЧНИХ СПОЛУК“. Bulletin of the Kyiv National University of Technologies and Design. Technical Science Series 126, Nr. 5 (12.02.2019): 114–22. http://dx.doi.org/10.30857/1813-6796.2018.5.13.

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Development of a method for evaluating the efficiency of decontamination in terms of the integral effects of the splitting of toxic substances on the human body. Paraoxon is the model substance of the characteristic chemical structure and toxicological characteristics. As a model system for determining the toxicity of paraoxone and its alkaline hydrolysis products, the inhibition of human serum butyrylcholinesterase was used. Determination of butyrylcholinesterase activity was performed ex vivo spectrophotometrically using the modified Ellman method.

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M. Schopfer, Lawrence, Emilie David, Steven H. Hinrichs und Oksana Lockridge. „Human butyrylcholinesterase in Cohn fraction IV-4 purified in a single chromatography step on Hupresin“. PLOS ONE 18, Nr. 1 (13.01.2023): e0280380. http://dx.doi.org/10.1371/journal.pone.0280380.

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Protection from the toxicity of nerve agents is achieved by pretreatment with human butyrylcholinesterase (BChE). Current methods for purifying large quantities of BChE from frozen Cohn fraction IV-4 produce 99% pure enzyme, but the yield is low (21%). Our goal was to simplify the purification procedure and increase the yield. Butyrylcholinesterase was extracted from frozen Cohn fraction IV-4 in 10 volumes of water pH 6. The filtered extract was pumped onto a Hupresin affinity column. The previously utilized anion exchange chromatography step was omitted. Solvent and detergent reagents used to inactivate lipid enveloped virus, bacteria and protozoa did not bind to Hupresin. BChE was eluted with 0.1 M tetramethylammonium bromide in 20 mM sodium phosphate pH 8.0. BChE protein was concentrated on a Pellicon tangential flow filtration system and demonstrated to be highly purified by mass spectrometry. A high pump rate produced protein aggregates, but a low pump rate caused minimal turbidity. Possible contamination by prekallikrein and prekallikrein activator was examined by LC-MS/MS and by a chromogenic substrate assay for kallikrein activity. Prekallikrein and kallikrein were not detected by mass spectrometry in the 99% pure BChE. The chromogenic assay indicated kallikrein activity was less than 9 mU/mL. This new, 1-step chromatography protocol on Hupresin increased the yield of butyrylcholinesterase by 200%. The new method significantly reduces production costs by optimizing yield of 99% pure butyrylcholinesterase.

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Gholivand, Khodayar, Mohammad Abdollahi, Fresia Mojahed, Ahlam Madani Alizadehgan und Gholamreza Dehghan. „Acetylcholinesterase/Butyrylcholinesterase inhibition activity of some new carbacylamidophosphate deriviatives“. Journal of Enzyme Inhibition and Medicinal Chemistry 24, Nr. 2 (01.04.2009): 566–76. http://dx.doi.org/10.1080/14756360802316971.

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Lampón, Natalia, Esperanza F. Hermida-Cadahia, Alberto Riveiro und J. Carlos Tutor. „Association between butyrylcholinesterase activity and low-grade systemic inflammation“. Annals of Hepatology 11, Nr. 3 (Mai 2012): 356–63. http://dx.doi.org/10.1016/s1665-2681(19)30932-9.

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Nechaeva, Natalia, Taisiya Prokopkina, Galina Makhaeva, Elena Rudakova, Natalia Boltneva, Christophor Dishovsky, Arkadiy Eremenko und Ilya Kurochkin. „Quantitative butyrylcholinesterase activity detection by surface-enhanced Raman spectroscopy“. Sensors and Actuators B: Chemical 259 (April 2018): 75–82. http://dx.doi.org/10.1016/j.snb.2017.11.174.

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Kálmán, János, Anna Juhász, Zoltán Rakonczay, György Ábrahám, Marianna Zana, Krisztina Boda, Tibor Farkas, Botond Penke und Zoltán Janka. „Increased serum butyrylcholinesterase activity in type IIb hyperlipidaemic patients“. Life Sciences 75, Nr. 10 (Juli 2004): 1195–204. http://dx.doi.org/10.1016/j.lfs.2004.02.019.

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BHARAJ, B., und H. ASEMOTA. „Liver and serum butyrylcholinesterase activity in scorbutic guinea pigs“. Journal of Nutritional Biochemistry 4, Nr. 2 (Februar 1993): 77–79. http://dx.doi.org/10.1016/0955-2863(93)90003-f.

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Vlaskin, D. N., E. T. Gainullina, S. B. Ryzhikov und V. F. Taranchenko. „Rapid Method for Diagnosis of Abnormal Activity of Butyrylcholinesterase“. Bulletin of Experimental Biology and Medicine 139, Nr. 2 (Februar 2005): 263–65. http://dx.doi.org/10.1007/s10517-005-0265-7.

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Chelminska-Bertilsson, Monika, Stig Allenmark und Lars Edebo. „Butyrylcholinesterase activity towards long-chain alkanoylcholines: kinetics and mechanism“. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1202, Nr. 1 (September 1993): 56–60. http://dx.doi.org/10.1016/0167-4838(93)90062-v.

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Farid, Ayman Samir, und Yoichiro Horii. „Nippostrongylus brasiliensis: Infection decreases plasma butyrylcholinesterase activity in rats“. Experimental Parasitology 122, Nr. 2 (Juni 2009): 162–64. http://dx.doi.org/10.1016/j.exppara.2009.02.009.

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ŠAGUD, Ivana, Irena ŠKORIĆ, Dragana VUK, Ana RATKOVIĆ und Franko BURČUL. „Acetyl- and butyrylcholinesterase inhibitory activity of selected photochemicallysynthesized polycycles“. TURKISH JOURNAL OF CHEMISTRY 43, Nr. 4 (06.08.2019): 1170–82. http://dx.doi.org/10.3906/kim-1903-74.

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Hou, Shurong, Liu Xue, Wenchao Yang, Lei Fang, Fang Zheng und Chang-Guo Zhan. „Substrate selectivity of high-activity mutants of human butyrylcholinesterase“. Organic & Biomolecular Chemistry 11, Nr. 43 (2013): 7477. http://dx.doi.org/10.1039/c3ob41713a.

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Alcântara, V. M., E. A. Chautard-Freire-Maia, M. Scartezini, M. S. J. Cerci, K. Braun-Prado und G. Picheth. „Butyrylcholinesterase activity and risk factors for coronary artery disease“. Scandinavian Journal of Clinical and Laboratory Investigation 62, Nr. 5 (Januar 2002): 399–404. http://dx.doi.org/10.1080/00365510260296564.

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Jasiecki, Jacek, Joanna Jońca, Monika Żuk, Anna Szczoczarz, Anna Janaszak-Jasiecka, Krzysztof Lewandowski, Krzysztof Waleron und Bartosz Wasąg. „Activity and polymorphisms of butyrylcholinesterase in a Polish population“. Chemico-Biological Interactions 259 (November 2016): 70–77. http://dx.doi.org/10.1016/j.cbi.2016.04.030.

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48

Kulhánková, Andrea, Lucie Cahlíková, Zdeněk Novák, Kateřina Macáková, Jiří Kuneš und Lubomír Opletal. „Alkaloids fromZephyranthes robustaBakerand Their Acetylcholinesterase- and Butyrylcholinesterase-Inhibitory Activity“. Chemistry & Biodiversity 10, Nr. 6 (Juni 2013): 1120–27. http://dx.doi.org/10.1002/cbdv.201200144.

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Meden, Anže, Damijan Knez, Natalia Malikowska-Racia, Xavier Brazzolotto, Florian Nachon, Jurij Svete, Kinga Sałat, Uroš Grošelj und Stanislav Gobec. „Structure-activity relationship study of tryptophan-based butyrylcholinesterase inhibitors“. European Journal of Medicinal Chemistry 208 (Dezember 2020): 112766. http://dx.doi.org/10.1016/j.ejmech.2020.112766.

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Hošt'álková, Anna, Lubomír Opletal, Jiří Kuneš, Zdeněk Novák, Martina Hrabinová, Jakub Chlebek, Lukáš Čegan und Lucie Cahlíková. „Alkaloids from Peumus boldus and their Acetylcholinesterase, Butyrylcholinesterase and Prolyl Oligopeptidase Inhibition Activity“. Natural Product Communications 10, Nr. 4 (April 2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000410.

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Eleven isoquinoline alkaloids (1–11) were isolated from dried leaves of Peumus boldus Mol. by standard chromatographic methods. The chemical structures were elucidated by MS, and 1D and 2D NMR spectroscopic analysis, and by comparison with literature data. Compounds isolated in sufficient amount were evaluated for their acetylcholinesterase, and butyrylcholinesterase inhibition activity using Ellman's method. In the prolyl oligopeptidase assay, Z-Gly-Pro- p-nitroanilide was used as substrate. Promising butyrylcholinesterase inhibition activities were demonstrated by two benzylisoquinoline alkaloids, reticuline (8) and N-methylcoclaurine (9), with IC50 values of 33.6 ± 3.0 μM and 15.0 ± 1.4 μM, respectively. Important prolyl oligopeptidase inhibition activities were shown by N-methyllaurotetanine (6) and sinoacutine (4) with IC50 values of 135.4 ± 23.2 μM and 143.1 ± 25.4 μM, respectively. Other tested compounds were considered inactive.

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