Journal of Neurochemistry · 1971 · 34 citations · 13 references
Life SciencesBiochemistryNeuroscienceEnzymologyNeurochemistryProtein BiochemistryCholinergic NeurochemistryLipid-protein InteractionsMembrane CharacterizationMembrane OrganizationMembrane ProteinsMembrane-bound EnzymesEnzyme-lipid InteractionsMembrane Protein SeparationMembrane Protein Solubilization
Abstract— 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.
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