Abstract
Release of iron from ferritin and deoxyribose degradation were caused by alloxan in the presence of reduced glutathione (GSH).Superoxide dismutase, catalase, diethylenetriaminepentaacetic acid and hydroxyl radical scavengers such as mannitol and benzoate inhibited the degradation of deoxyribose in the alloxan-GSH system, suggesting that hydroxyl radical was generated in the alloxan-GSH system in the presence of ferritin.Iron released from ferritin may catalyze hydroxyl radical generation via the Haber Weiss reaction.However, the inhibition of the iron release from ferritin in the alloxan-GSH system required a large amount of superoxide dismutase.These results suggest that the iron release from ferritin in the alloxan-GSH system is not primarily due to superoxide.These findings may help to explain the precise mechanism of alloxan toxicity.
