نتایج جستجو برای: benzoheterocycles butyrylcholinesterase

تعداد نتایج: 1364  

Journal: :Collegium antropologicum 2004
Branka Surina Drazen Nosso Zoran Siftar Zlata Flegar-Mestrić Vera Simeon-Rudolf

Recognition of butyrylcholinesterase (EC 3.1.1.8) variants in human serum is essential to identify patients who may be susceptible to a prolonged reaction of suxamethonium and mivacurium, short-acting muscle relaxants. Thus they can be given appropriate advice along with their relatives who may be similarly affected. Therefore, Cholinesterase Unit for detection of individuals, carriers of inher...

Journal: :Molecular pharmacology 1998
A Saxena Y Ashani L Raveh D Stevenson T Patel B P Doctor

To understand the role of glycosylation in the circulation of cholinesterases, we compared the mean residence time of five tissue-derived and two recombinant cholinesterases (injected intravenously in mice) with their oligosaccharide profiles. Monosaccharide composition analysis revealed differences in the total carbohydrate, galactose, and sialic acid contents. The molar ratio of sialic acid t...

Journal: :Genomics 1991
P W Allderdice H A Gardner D Galutira O Lockridge B N LaDu P J McAlpine

Human tissues have two distinct cholinesterase activities: acetylcholinesterase and butyrylcholinesterase. Acetylcholinesterase functions in the transmission of nerve impulses, whereas the physiological function of butyryl-cholinesterase remains unknown. An atypical form of butyrylcholinesterase or the absence of its activity leads to prolonged apnea following administration of the muscle relax...

Journal: :Molecules 2017
Xavier Brazzolotto Alexandre Igert Virginia Guillon Gianluca Santoni Florian Nachon

Human butyrylcholinesterase is a performant stoichiometric bioscavenger of organophosphorous nerve agents. It is either isolated from outdated plasma or functionally expressed in eukaryotic systems. Here, we report the production of active human butyrylcholinesterase in a prokaryotic system after optimization of the primary sequence through the Protein Repair One Stop Shop process, a structure-...

Journal: :Scandinavian journal of clinical and laboratory investigation 2011
Ronan M G Berg Keren Ofek Tavs Qvist Flemming Tofteng Hermona Soreq Kirsten Møller

BACKGROUND The circulating cholinesterases acetyl- and butyrylcholinesterase may be suppressed and subsequently released from the brain in acute bacterial meningitis. METHODS We report serum activities of acetylcholinesterase and butyrylcholinesterase in paired arterial and jugular venous samples from seven patients with acute bacterial meningitis and eight healthy controls. Paraoxonase 1, wh...

2013
Gang Zhou Gopal K. Marathe Jaana Hartiala Stanley L. Hazen Hooman Allayee W. H. Wilson Tang Thomas M. McIntyre

Background: Aspirin use is extensive, but its short half-life limits bioavailability. Results: Butyrylcholinesterase and PAFAH1b2 hydrolyze aspirin in plasma. Aspirin hydrolysis in plasma varies up to 12-fold from non-genetic modulation of butyrylcholinesterase activity. Conclusion: Two enzymes hydrolyze aspirin in plasma and their contribution varies among individuals. Significance: Aspirin hy...

2013
Brian C. Geyer Katherine E. Larrimore Jacquelyn Kilbourne Latha Kannan Tsafrir S. Mor

BACKGROUND Concerns about the safety of paralytics such as succinylcholine to facilitate endotracheal intubation limit their use in prehospital and emergency department settings. The ability to rapidly reverse paralysis and restore respiratory drive would increase the safety margin of an agent, thus permitting the pursuit of alternative intubation strategies. In particular, patients who carry g...

Journal: :Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie 1988
T Thomsen H Kewitz O Pleul

In vivo effects of reversible inhibitors of cholinesterase activity were determined radiometrically in undiluted samples of erythrocytes and plasma. [14C]acetylcholine at substrate saturation, 25 degrees C and pH 7.4 permitted rapid and precise determination of butyrylcholinesterase (EC 3.1.1.8) and acetylcholinesterase (EC 3.1.1.7) activities. Reference values for acetylcholinesterase and buty...

Journal: :Investigative ophthalmology & visual science 1992
R Salceda G Sánchez J M León-Cázares

This report presents a comparative description of the acetylcholinesterase and butyrylcholinesterase activities and their molecular forms in primary cultures of retinal pigment epithelium (RPE). Acetylcholinesterase activity increases during differentiation of the cells. Sucrose sedimentation analysis of acetylcholinesterase and butyrylcholinesterase molecular forms revealed the presence of A12...

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