Abstract
Yeast enolase, void of both sulfhydryl groups and disulfide bonds, rabbit muscle enolase, which contains sulfhydryl groups, and lactic dehydrogenase (LDH), which has a sulfhydryl group in the active site, were found to give similar ionic yields when irradiated with γ-radiation. Cysteine and 2-mercaptoethylguanidine (MEG), two sulfhydryl compounds, protected these three enzymes against ionizing radiations. It is concluded from this study that the presence of sulfhydryl groups in enzymes is not a reliable means of predicting radiation sensitivity, and sulfhydryl protective agents can function without the presence of a sulfhydryl or disulfide bond in the enzyme. It is suggested that the initial event in the radiation damage to proteins may be the breaking of H-bonds and thus the destruction of tertiary structure.
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