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THE DISSOCIATION OF RAT BRAIN MEMBRANES BEARING ACETYLCHOLINESTERASE BY THE NON‐IONIC DETERGENT TRITON X‐100 AND AN EXAMINATION OF THE PRODUCT
Author(s) -
Crone H. D.
Publication year - 1971
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.1471-4159.1971.tb11976.x
Subject(s) - membrane , acetylcholinesterase , chemistry , solubility , dissociation (chemistry) , triton x 100 , aché , enzyme , solubilization , chromatography , biochemistry , biophysics , pulmonary surfactant , organic chemistry , biology
— The action of Triton X‐100 on a membrane preparation from rat brain was studied with reference to the solubilization of acetylcholinesterase and the product was characterized by exclusion chromatography. The AChE and membrane protein were readily solubilized to form particles corresponding to a mol. wt. of about 5 × 10 5 . The solubility of these particles depended on the continued presence of the detergent. It was concluded that these soluble particles formed an intermediate stage in organization between membrane‐bound AChE and the soluble protein enzyme, and perhaps represented preexisting lipoprotein subunits of the membranes.