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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1985 Aug;82(16):5357–5359. doi: 10.1073/pnas.82.16.5357

Radiation inactivation of ricin occurs with transfer of destructive energy across a disulfide bridge.

H T Haigler, D J Woodbury, E S Kempner
PMCID: PMC390567  PMID: 3860867

Abstract

The ionizing radiation sensitivity of ricin, a disulfide-linked heterodimeric protein, was studied as a model to determine the ability of disulfide bonds to transmit destructive energy. The radiation-dependent loss of A chain enzymatic activity after irradiation of either intact ricin or ricin in which the interchain disulfide bond was disrupted gave target sizes corresponding to the molecular size of dimeric ricin or monomeric A chain, respectively. These results clearly show that a disulfide bond can transmit destructive energy between protein subunits.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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