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- W2022506890 abstract "Synaptic fractions of decreasing morphological complexity were prepared by phase partitioning of synaptic membranes in an aqueous two-phase polymer system containing increasing concentrations of the neutral detergent n-octyglucoside (OG). The morphology, distribution of concanavalin A binding sites (CABS) and protein and glycoprotein composition of the resultant fractions were examined. The lowest concentration of OG employed (0.5% w/w) gave fractions enriched in relatively intact junctions retaining both pre- and postsynaptic structures. Increasing the detergent concentration resulted in the stepwise solubilization of pre- and postsynaptic structures until purified postsynaptic densities (PSDs) were obtained with 1% (w/w) OG. CABS were generally distributed on all membrane structures present in the 0.5% OG fraction, were restricted to synaptic structures in the fraction obtained with 0.75% OG, and were localized to the convex (outer) surface of purified PSDs. Gel electrophoretic analysis showed that the restriction of CABS to the region of the synapse was associated with a marked increase in the concentration of glycoproteins with apparent molecular weights of 180,000 and 130,000. These glycoproteins were retained, and further concentrated in the purified PSD fraction." @default.
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- W2022506890 date "1983-10-01" @default.
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- W2022506890 title "Identification and localization of concanavalin A binding sites on isolated postsynaptic densities" @default.
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- W2022506890 doi "https://doi.org/10.1016/0006-8993(83)90555-3" @default.
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