Removal of ferritin‐bound iron by DL‐dihydrolipoate and DL‐dihydrolipoamide

FEBS Journal - Tập 155 Số 2 - Trang 295-300 - 1986
Francesco Bonomi1, Silvia Pagani1
1Institute of Biochemistry and of Chemistry, University of Milan

Tóm tắt

The naturally occurring dithiols DL‐dihydrolipoate and DL‐dihydrolipoamide were tested for their ability in the removal of ferritin‐bound iron. Both compounds remove the iron stored inside the protein by complexing it in the ferric form. The iron can be reduced to the ferrous form by excess dithiol, but this is not necessary for complete removal. Reaction is complete in few hours and, at molar ratios of chelator to metal higher than 10, more than 60% of the ferritin‐bound iron was removed. The amount of iron stored in the ferritin molecule does not affect the rate and the yield of the removal reaction.The iron‐removing ability of DL‐dihydrolipoate was found to be identical to that of an equimolar solution of sodium dithionite, and to be pH‐dependent.Results are discussed in terms of the molecular architecture of ferritin and of the chelators, and their possible physiological relevance is pointed out.

Từ khóa


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Thông tin
Thông tin xuất bản

FEBS Journal

Tập 155 Số 2

295-300

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