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- W1562668908 abstract "The purification of the enzyme acetylcholinesterase (EC 3.1.1.7) has attracted much attention because it was first recognized to be involved in nervous function. The study of acetylcholinesterase was facilitated by Nachmansohn's introduction of the electric organ of Electrophorus electrophorus as a source of the enzyme. Rothenberg and Nachmansohn using ammonium sulfate fractionation obtained a preparation that is now known to have been about 70% pure. This enzyme preparation had a very high molecular weight that was estimated at about 3×106. Kremzner and Wilson described a chromatographic technique for purifying this enzyme, using benzylated DEAE-Sephadex gel in an attempt at affinity chromatography. Although effective in purifying the enzyme this gel did not function as an affinity support. This enzyme preparation was nearly pure, had a low molecular weight of about 2.4×105, and behaved like a globular protein." @default.
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- W1562668908 date "1974-01-01" @default.
- W1562668908 modified "2023-09-23" @default.
- W1562668908 title "[74] A covalent affinity technique for the purification of all forms of acetylcholinesterase" @default.
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- W1562668908 doi "https://doi.org/10.1016/s0076-6879(74)34077-3" @default.
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