Published August 1985
| Version v1
Journal article
Radiation inactivation of ricin occurs with transfer of destructive energy across a disulfide bridge
Description
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
Additional details
Publishing Information
- Journal Title
- Proc. Natl. Acad. Sci. U.S.A
- Journal Volume
- 82
- Journal Issue
- 16
- Series
- Proc. Natl. Acad. Sci. U.S.A.
- Journal Page Range
- 5357-5359
- ISSN
- 0027-8424
- CODEN
- PNASA
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 17042964
- Subject category
- S38: RADIATION CHEMISTRY, RADIOCHEMISTRY AND NUCLEAR CHEMISTRY;
- Descriptors DEI
- CHEMICAL RADIATION EFFECTS; ELECTRON BEAMS; INACTIVATION; LECTINS; MEV RANGE 10-100; PROTEINS; TRITIUM COMPOUNDS
- Descriptors DEC
- BEAMS; ENERGY RANGE; HYDROGEN COMPOUNDS; LEPTON BEAMS; MEV RANGE; ORGANIC COMPOUNDS; PARTICLE BEAMS; RADIATION EFFECTS