Nine sites of oxidized insulin B-chain were cleaved by phytolacain R, isolated from pokeweed, after 20 hr of hydrolysis. Five cleavage sites resembled those of papain. Substrate specificity of phytolacain R was similar to that of papain, preferring hydrophobic P2residues. The activities of fibrin formation and elastin hydrolysis of phytolacain R were higher than those of papain. The amino terminal sequence of phytolacain R, although similar was not identical with that of papain. © 1995.
Kaneda, M., Nagatome, S., & Uchikoba, T. (1995). Comparison of phytolacain R, a cysteine protease from Phytolacca americana, with papain. Phytochemistry, 39(5), 997–999. https://doi.org/10.1016/0031-9422(95)00163-2