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• W1963669822 startingPage "2748" @default.
• W1963669822 abstract "The carbohydrate-binding protein, Concanavalin A (Con A), binds to glucose- or mannose-like sites on the cell-surface membrane. Unless the cells are treated with trypsin, this protein agglutinates malignantly transformed cells, but not normal cells. The transformed cells were agglutinated at 24°C but not at 4°C. Transformed and normal cells treated with trypsin were agglutinated at both 24°C and 4°C with high concentrations of Con A (500 μg/ml), but only at 24°C with low concentrations (5 μg/ml). The same number of Con A molecules were bound to normal and transformed cells at both temperatures. The results indicate that the site for Con A on the surface membrane contains two activities, a component that binds Con A molecules ( B ) and a component that determines agglutination ( A ). B is not temperature sensitive and is active in normal and transformed cells, whereas A , which is temperature sensitive, is in an active form only in transformed cells. A can be activated by trypsin, and the increased activity per cell allows agglutination at 4°C with a high, but not with a low, concentration of Con A. Agglutination of transformed cells by wheat-germ agglutinin, which binds to N -acetyl-D-glucosamine-like sites, and by soybean agglutinin, which binds to N -acetyl-D-galactosamine-like sites, was not temperature sensitive. Thus, the temperature-sensitive component A is specific for Con A, and malignant transformation of normal cells, which results in agglutinability by Con A, is associated with the activation of a specific temperature-sensitive activity on the surface membrane." @default.
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• W1963669822 date "1971-11-01" @default.
• W1963669822 modified "2023-09-27" @default.
• W1963669822 title "A Specific Metabolic Activity on the Surface Membrane in Malignant Cell-Transformation" @default.
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• W1963669822 doi "https://doi.org/10.1073/pnas.68.11.2748" @default.
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