Interaction of ricin and its constituent polypeptides with dipalmitoylphosphatidylcholine vesicles

24Citations
Citations of this article
2Readers
Mendeley users who have this article in their library.
Get full text

Abstract

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.

Cite

CITATION STYLE

APA

Utsumi, T., Aizono, Y., & Funatsu, G. (1984). Interaction of ricin and its constituent polypeptides with dipalmitoylphosphatidylcholine vesicles. BBA - Biomembranes, 772(2), 202–208. https://doi.org/10.1016/0005-2736(84)90045-2

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free