Modeccin, the toxin of Adenia digitata. Purification, toxicity and inhibition of protein synthesis in vitro

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Abstract
Modeccin, the toxin of A. digitata (Modecca digitata), was purified from the roots of this plant by affinity chromatography on Sepharose 4B. This toxin is a protein with MW 57,000, which on treatment with 2-mercaptoethanol is dissociated into 2 subunits of MW 25,000 and 32,000. Modeccin inhibits protein synthesis in vitro in a lysate of rabbit reticulocytes and in Ehrlich ascites cells the effect on cells is decreased in the presence of lactose. Dissociation of modeccin into subunits decreases the toxicity to animals and the inhibition of protein synthesis in cells, but enhances the inhibition of protein synthesis in the lysate system.

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