RT Journal Article SR Electronic(1) A1 Yamamoto, YokoYR 1979 T1 Two Molecular Species of Mouse L Cell Interferon Differing in Lectin Binding JF Journal of General Virology, VO 42 IS 3 SP 533 OP 539 DO https://doi.org/10.1099/0022-1317-42-3-533 PB Microbiology Society, SN 1465-2099, AB SUMMARY 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. 24000) and S (mol. wt. 36000), 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 α-methyl-d-glucoside, indicating that at least some of the F species are also glycoprotein, and that both F and S interferons are heterogeneous as regards their affinity to this lectin., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-42-3-533