title: Purification and characterization of a toxin inhibiting protein synthesis from Croton mongue, a Madagascar Euphorbiaceae.
abstract: Monguine, a thermostable toxic protein was extracted from the seeds of Croton mongue (Euphorbiaceae) and purified by ion-exchange chromatography on DEAE-cellulose and gel filtration on Sephadex G-25 and G-15. Polyacrylamide gel electrophoresis of purified monguine in the presence of sodium dodecyl sulfate and after treatment with 2-mercaptoethanol showed one band corresponding to a molecular weight of 9000. The same molecular weight was determined by analytical centrifugation. Amino acid analysis revealed a high content in both aspartic and glutamic acids (or the corresponding amides). The LD50 (24 h) is 12 mg/kg of mouse body weight. Monguine inhibits protein synthesis in hepatoma tissue culture cells and globin synthesis in a rabbit reticulocyte lysate.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001681:Biological Assay; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D007928:Lethal Dose 50; D008114:Liver Neoplasms, Experimental / Q000378:metabolism; D008297:Male; D051379:Mice; D014176:Protein Biosynthesis; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D012639:Seeds / Q000032:analysis*; D014118:Toxins, Biological / Q000302:isolation & purification* / Q000494:pharmacology / Q000633:toxicity
chemical_list: D000596:Amino Acids; D014118:Toxins, Biological; C051089:monguine