Modeccin, the toxin of Adenia digitata. Purification, toxicity and inhibition of protein synthesis in vitro

Biochem J. 1978 Aug 15;174(2):491-6. doi: 10.1042/bj1740491.

Abstract

1. Modeccin, the toxin of Adenia digitata (Modecca digitata), was purified from the roots of this plant by affinity chromatography on Sepharose 4B. 2. This toxin is a protein with mol.wt. 57000, which on treatment with 2-mercaptoethanol can be dissociated into two subunits of mol.wts. 25000 and 32000. 3. Modeccin inhibits protein synthesis in vitro in a lysate of rabbit reticulocytes and in Ehrlich ascites cells; the effect on cells is decreased in the presence of lactose. 4. Dissociation of modeccin into subunits decreases the toxicity to animals and the inhibition of protein synthesis in cells, but enhances the inhibition of protein synthesis in the lysate system.

MeSH terms

  • Animals
  • Chemical Phenomena
  • Chemistry
  • Chromatography, Agarose
  • Electrophoresis, Polyacrylamide Gel
  • In Vitro Techniques
  • Lactose / pharmacology
  • Lectins / isolation & purification*
  • Male
  • Mice
  • Molecular Weight
  • Plant Lectins
  • Plants, Toxic* / analysis
  • Protein Biosynthesis
  • Rats
  • Ribosome Inactivating Proteins, Type 2
  • Toxins, Biological* / isolation & purification
  • Toxins, Biological* / pharmacology
  • Toxins, Biological* / toxicity

Substances

  • Lectins
  • Plant Lectins
  • Ribosome Inactivating Proteins, Type 2
  • Toxins, Biological
  • modeccin
  • Lactose