Radiation inactivation of ricin occurs with transfer of destructive energy across a disulfide bridge.
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.
D004220:Disulfides / Q000528:radiation effects; D007700:Kinetics; D046911:Macromolecular Substances; D011487:Protein Conformation; D011489:Protein Denaturation; D012276:Ricin / Q000378:metabolism / Q000528:radiation effects*
D004220:Disulfides; D046911:Macromolecular Substances; D012276:Ricin