Interaction of ricin and its constituent polypeptides with dipalmitoylphosphatidylcholine vesicles

  • Utsumi T
  • Aizono Y
  • Funatsu G
  • 2


    Mendeley users who have this article in their library.
  • 24


    Citations of this article.


The interaction of ricin and of its constituent polypeptides, the A- and B-chain, with dipalmitoylphosphatidylcholine (DPPC) vesicles was investigated. The A- and B-chain were individually associated with DPPC vesicles, although the intact ricin was not associated. The maximum binding and association constants were evaluated to be 154 μg per mg of DPPC and Ka2.30 · 105M-1for the A-chain, and 87 μg per mg of DPPC and Ka14.5 · 105M-1for the B-chain, respectively. The A-chain could induce the phase transition release of carboxyfluorescein from DPPC vesicles to a greater extent than the B-chain, whereas the release induced by the intact ricin was negligible. The evidence indicated that the hydrophobic regions on the A-chain and on the B-chain were buried inside when the two chains constituted the intact ricin molecule through one interchain disulfide bond, and that the A-chain caused perturbation of the DPPC bilayer at the phase transition temperature with consequent leakage of carboxyfluorescein. © 1984.

Author-supplied keywords

  • Membrane-protein interaction
  • Phase transition
  • Phospholipid vesicle
  • Ricin

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free