Abstract
Abstract The radiolytic degradation of proteins in oxygenated solution is initiated by the attack of OH radicals at a multiplicity of main-chain and side-chain loci to give a wide variety of oxidized protein sites. A major fraction of these oxidation reactions lead to the introduction of reactive carbonyl groups into the protein co-valent structure. With γ-rays the total carbonyl yield correspond to G(>CO)t ≃ 1 for a number of different proteins. Outlined here is a sensitive chemical-spectrophotometric procedure for quantitatively monitoring G(>CO)t over a dose range of interest in radiation biology (1 to 50 Krad). Data obtained with pepsin, α-chymotryps in and β-lactoglobulin are discussed.
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