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- W3035905916 abstract "Scanning electron microscopy has been applied to study the surface ultrastructure of the Golgi complex and labelling techniques have been developed to investigate the distribution of lectin-binding sites on the membrane surfaces. The study is based on the examination of Golgi-rich fractions, isolated by homogenisation and differential centrifugation of rat liver. The membranes are fixed in suspension with 1% glutaraldehyde in 0.1 M sodium phosphate buffer, pH 7.4 for 60 mins and then rinsed in distilled water. For scanning electron microscopy, a thin film of membrane is frozen rapidly on coverglasses using liquid Freon 22, cooled by liquid nitrogen and dried in vacuo at -60°C. Membranes are coated with approximately 100 Å gold in a sputter coater and examined at 20 kV in a JEOL JSM-35U scanning electron microscope. For transmission electron microscopy, membranes are processed as described previously. For examination of lectin binding sites, isolated Golgi membranes are washed in sodium bicarbonate buffer, fixed in glutaraldehyde, incubated with concanavalin A (Con A), rinsed in buffer and then incubated with hemocyanin1." @default.
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- W3035905916 date "1978-08-01" @default.
- W3035905916 modified "2023-09-26" @default.
- W3035905916 title "Surface structure of the golgi complex and identification of concanavalin-A binding sites" @default.
- W3035905916 doi "https://doi.org/10.1017/s0424820100082091" @default.
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