The intersubunit disulfide bridge of ricin is essential for cytotoxicity

Arch Biochem Biophys. 1987 Jul;256(1):280-4. doi: 10.1016/0003-9861(87)90447-4.

Abstract

Alkylation of the cysteine residues which link the A and B chains of ricin through a disulfide bridge produces a molecule which still binds to HeLa cells and is toxic toward in vitro ribosome-directed translation, but which has little or no cytotoxicity toward cells in culture. This and similar observations on diphtheria toxin implicate the intersubunit disulfide bridge in the transport of the toxic subunits of these toxins into the cytoplasm.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alkylation
  • Animals
  • Autoradiography
  • Binding Sites
  • Chromatography, High Pressure Liquid
  • Disulfides / analysis*
  • HeLa Cells
  • Humans
  • In Vitro Techniques
  • Protein Biosynthesis
  • Rabbits
  • Ricin / metabolism
  • Ricin / toxicity*

Substances

  • Disulfides
  • Ricin