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TRITON SOLUBILIZED ACETYLCHOLINESTERASE OF BRAIN
Author(s) -
Ho I. K.,
Ellman G. L.
Publication year - 1969
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1969.tb09905.x
Subject(s) - acetylthiocholine , acetylcholinesterase , protease , chemistry , chromatography , aché , enzyme , venom , hydrolysis , solubilization , brain tissue , biochemistry , triton x 100 , specific activity , biology , pulmonary surfactant , anatomy
—The total AChE of brain can be readily extracted into aqueous Triton X‐100. By column chromatography of these extracts a preparation was obtained at least six times as active as the original material and in yields of 60‐80 per cent of the original amounts. The molecular weight of this material was estimated to be over 200,000. When brain tissue was treated with venom or bacterial protease, a water‐soluble AChE was obtained with an overall purification of 150‐fold. The most active preparation of AChE hydrolysed 880 μ‐moles of acetylthiocholine/hr/mg of protein. The molecular weight of this preparation was estimated to be about 100,000. The enzyme which was extracted by Triton X‐100 is probably the precursor of the more water‐soluble enzyme that can be prepared from brain tissue by treatment with venom or protease.