Abstract
Binding of L cell interferon to lectins, Wistaria floribunda agglutinin (WFA) and concanavalin A (Con A) was studied by affinity chromatography. Of the two molecular species of L cell interferon, F (mol. wt. 24,000) and S (mol. wt. 36,000), only the latter was bound efficiently to WFA-Sepharose and eluted quantitatively with D-galactose followed by a pH 3 buffer, suggesting a substantial difference between the two interferon species in their carbohydrate structure. Both were partially bound to Con A-Sepharose and eluted with alpha-methyl-D- glucoside, indicating that at least some of the F species are also glycoprotein, and that both F and S interferon are heterogeneous as regards their affinity to this lectin.