Multiple Molecular Forms of Purified Human Erythrocyte Acetylcholinesterase
نویسندگان
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...
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Membrane bound, Triton X-100 solubilized bovine nucleus caudatus acetylcholinesterase is sedimenting in presence of Triton X-100 concentrations higher than the CMC as a 10.5 S-detergent-enzyme complex. There is evidence that this complex does neither represent the molecular enzyme arrangement present in the membrane, nor the molecular form originally released from the membrane. The purified, cy...
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...
متن کاملHuman Erythrocyte Acetylcholinesterase in Health and Disease.
The biochemical properties of erythrocyte or human red blood cell (RBC) membrane acetylcholinesterase (AChE) and its applications on laboratory class and on research are reviewed. Evidence of the biochemical and the pathophysiological properties like the association between the RBC AChE enzyme activity and the clinical and biophysical parameters implicated in several diseases are overviewed, an...
متن کاملCellular localization of the multiple molecular forms of acetylcholinesterase in cultured neuronal cells.
The cellular localization of the molecular forms of acetylcholinesterase was explored in chick sympathetic neurons and in mouse T28 cells (neuroblastoma X sympathetic ganglion cell hybrids) using the reversible, poorly lipid-soluble inhibitor of acetylcholinesterase, BW284C51, to protect cell surface activity while inactivating cytoplasmic activity with DFP, an irreversible, lipid-soluble inhib...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1975
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1975.tb02322.x