Quantitative Binding of 125I-Concanavalin A to Normal and Transformed Cells

AUTOR(ES)

Arndt-Jovin, Donna J.

RESUMO

We have measured the quantitative binding of the radioactively labeled agglutinin 125I-concanavalin A to normal mammalian cells and simian virus 40- and polyoma virus-transformed cells from tissue culture. Parallel measurements of the amount of 125I-concanavalin A necessary to cause agglutination of the cells in suspension were carried out. The transformed and nontransformed cells used for these experiments show large differences in their ability to be agglutinated by 125I-concanavalin A. However, these cell lines have the same number of specific binding sites and similar affinities for the agglutinin whether transformed, trypsinized, or nontransformed. We conclude that the differential capacity of concanavalin A to agglutinate transformed cells relative to normal cells does not result from differences in the number of binding sites between the two types of cells.

Documentos Relacionados

• INTERACTION OF THE CARBOHYDRATE-BINDING PROTEIN CONCANAVALIN A WITH NORMAL AND TRANSFORMED CELLS
• Differences in the Binding of Fluorescent Concanavalin A to the Surface Membrane of Normal and Transformed Cells
• A Comparative Evaluation of the Distribution of Concanavalin A-Binding Sites on the Surfaces of Normal, Virally-Transformed, and Protease-Treated Fibroblasts
• Binding and internalization of thrombin by normal and transformed chick cells.
• Occurrence of caldesmon (a calmodulin-binding protein) in cultured cells: Comparison of normal and transformed cells