Abstract
THE carbohydrate binding protein concanavalin A (Con A)1–3 can agglutinate cells transformed by a variety of carcinogenic agents, but it only agglutinates normal cells after they have been treated with trypsin4. This agglutination was reversed by competition with α-methyl-D-glucopyranoside (α-MG). These results indicated that transformed cells contain exposed binding sites that interact with Con A, whereas most such sites on normal cells are in a cryptic form4,5. These experiments were undertaken to determine whether treatment with Con A can result in cell toxicity; and if so, whether the difference in structure of the surface membrane between normal and transformed cells can result in a differential toxic effect, and can be used to inhibit tumour development in vivo.
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