Multiple forms of acetylcholinesterase from human erythrocytes
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چکیده
منابع مشابه
Multiple forms of acetylcholinesterase from human erythrocytes.
1. Acetylcholinesterase from human erythrocytes was solubilized with Triton X-100 in strong salt solution and partially purified by (NH(4))(2)SO(4) fractionation. This preparation showed three main bands of enzyme activity after electrophoresis on polyacrylamide gel and incubation with either alpha-naphthyl acetate or acetylthiocholine as enzyme substrate. Two of the multiple forms were complet...
متن کاملMultiple 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...
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Glycocholate and taurocholate have been shown (Coleman & Holdsworth, 1976; Billington & Coleman, 1978) to release significant amounts of membrane proteins and phospholipid from erythrocytes before the occurrence of significant cell lysis. Our particular interest was to study in detail the release of acetylcholinesterase from human erythrocytes. Heparinized human blood was centrifuged at 2500g f...
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Lead induced neurotoxicity in the people engaged in different occupations has received wide attention but very little studies have been carried out to monitor occupational neurotoxicity directly due to lead exposure using biochemical methods. In the present paper an endeavour has been made in order to assess the lead mediated neurotoxicity by in vitro assay of the activity of acetylcholinestera...
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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 ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1973
ISSN: 0264-6021
DOI: 10.1042/bj1330521