Has N-glycosidase activity and is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing a specific adenine of 28S rRNA (PubMed:14686924, PubMed:3932357, PubMed:2930482, PubMed:16997573). Inhibits GTP-dependent binding of EF2 (elongation factor 2) to ribosomes (PubMed:2930482). Binds to cell receptors and probably facilitates the entry into the cell of the A chain (By similarity). Acts also as a galactose-specific lectin responsible for cell agglutination (PubMed:3932357, PubMed:16997573). Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. Hemagglutinating activity is inhibited by galactose and structurally related sugars. Loss of protein synthesis inhibiting activity of the rabbit reticulocyte lysate by heating at 70 degrees Celsius for 20 minutes. The inhibitory activity of the solution is almost completely lost after storage for 2 weeks at 4 degrees Celsius in the presence of 1% 2-mercaptoethanol. Disulfide-linked dimer of A and B chains. Expressed in roots (at protein level) (PubMed:14686924, PubMed:3932357, PubMed:16997573, PubMed:19591862). Expressed in seeds (at protein level) (PubMed:3932357). N-glycosylated. Contains mannose and galactose. The measured mass is that of the reduced form. Causes an allergic reaction in human. Natural protein was found to bind to IgE of a patient who had been working with ribosome-inactivating proteins for two years in a research laboratory setting. LD(50) is 0.32 ug/kg by intraperitoneal injection into rats (at 48 hours post-injection). LD(50) is 1.73 ug/kg by intraperitoneal injection into mice (at 48 hours post-injection). LD(50) is 0.061 ug/kg by intraperitoneal injection into rats (at 14 days post-injection). LD(50) is 1.38 ug/kg by intraperitoneal injection into mice (at 14 days post-injection). In the N-terminal section; belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.