Abstract
Reduced coenzymes protected trypsin against inactivation to a greater extent than did oxidized coenzymes, both in dilute solution and dry state. The protective effect of oxidized coenzymes was almost independent of oxygen, whereas the protective effect of the reduced coenzymes was much greater in the absence than in the presence of oxygen. Electron spin resonance spectro-scopy showed that radicals formed in reduced coenzymes irradiated in the dry state were more stable than those induced in oxidized coenzymes. Molecular mixtures of macromolecules and NADH2 irradiated at 77[degree]K and heat-treated to room temperature produced a higher total number of radicals than calculated from the components irradiated separately. Data that a transfer of unpaired spins may occur from macromolecules to NADH2. Data are compatible with the view that NADH2 and NADPH2 may participate in the repair of target radicals in irradiated cells by hydrogen transfer mechanism.