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

Journal Article · Thu Aug 01 00:00:00 EDT 1985 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.82.16.5357· OSTI ID:6344130

Haigler, H T; Woodbury, D J; Kempner, E S

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.

• Research Organization: Univ. of California, Irvine
• OSTI ID: 6344130
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 82:16; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

38 RADIATION CHEMISTRY, RADIOCHEMISTRY, AND NUCLEAR CHEMISTRY
400600* -- Radiation Chemistry
BEAMS
CHEMICAL RADIATION EFFECTS
CHEMISTRY
ELECTRON BEAMS
ENERGY RANGE
INACTIVATION
LABELLED COMPOUNDS
LECTINS
LEPTON BEAMS
MEV RANGE
MEV RANGE 10-100
ORGANIC COMPOUNDS
PARTICLE BEAMS
PROTEINS
RADIATION CHEMISTRY
RADIATION EFFECTS
TRITIUM COMPOUNDS