Active-site determinations on forms of mammalian brain and eel acetylcholinesterase
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منابع مشابه
Multiple forms of acetylcholinesterase from pig brain.
1. A number of methods of solubilization of pig brain acetylcholinesterase (EC 3.1.1.7) were studied. The multiple enzymic forms of the resultant preparations were examined by polyacrylamide-gel electrophoresis. 2. Butanol extraction, Nagarase treatment and ultrasonication proved unsuitable as preparatory methods, but detergent treatment (Triton X-100, Triton X-100-KCl and lysolecithin) gave go...
متن کاملAnalysis of the forms of acetylcholinesterase from adult mouse brain.
The solubilization of 80% of the acetylcholinesterase activity of mouse brain was performed by repeated 2h incubations of homogenates at 37 degrees C in an aqueous medium. Analysis of the soluble extract by gel filtration on Sephadex G-200 showed that up to 80% of the enzyme activity was eluted in a peak which was estimated to consist of molecules of about 74000mol.wt. This peak was called the ...
متن کامل1-Bromopinacolone, an active site-directed covalent inhibitor for acetylcholinesterase.
1-Bromopinacolone, BrPin, acts initially as a reversible competitive inhibitor for acetylcholinesterase, KI = 0.18 mM in hydrolysis of acetylcholine. Unlike bromoacetone, with time it acts as an irreversible covalent inhibitor. BrPin has a hydrolytic half-life of 30 h at the pH of incubation, 7.8. The enzyme-BrPin complex is 50% inactivated in 2 h. First order kinetics are observed; the rate co...
متن کاملPurification by affinity chromatography of the molecular forms of acetylcholinesterase present in fresh electric-organ tissue of electric eel.
An acetylcholinesterase inhibitor-Sepharose conjugate was prepared by coupling a derivative of the powerful acetylcholinesterase inhibitor, N-methylacridinium, to CNBr-activated Sepharose. Use of this conjugate permitted direct purification, by affinity chromatography, of the two molecular forms of acetylcholinesterase, 14 and 18 S, present in fresh electric organ tissue. The purified 14S and 1...
متن کاملThe Electronic Influence on the Active Site-Directed Inhibition of Acetylcholinesterase by N-aryl-Substituted Succinimides
A computational docking approach, in combination with the Hammett relationship, has been employed to evaluate the electronic influence of substituents on ligand binding and the active site-directed inhibitory potency on acetylcholinesterase using nine N-aryl-substituted succinimides. Our results indicate that electronwithdrawing groups attached to benzene moiety of the compounds favor the inhib...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1976
ISSN: 0264-6021
DOI: 10.1042/bj1570069