منابع مشابه
BINDING OF Fe2+ BY MAMMALIAN FERRITIN
An average of 140 Fe 2 + ions bind to mammalian ferritin that has an average core content of 1876 Fe+ ions per molecule. The Fe2+ ions enter the protein interior and exchange electrons with the core Fe+ ions. A non-homogeneous model for the iron-eontaining core of ferritin is proposed.
متن کاملReduction of mammalian ferritin.
Mammalian ferritin from horse spleen undergoes an electrochemical or chemical reduction reaction in which each iron atom present is reduced by one electron (2300 electrons per ferritin molecule containing 2300 Fe3+ ions). Midpoint potentials of -190 mV, -310 mV, and -416 mV were determined at pH 7.0, 8.0, and 9.0. This variation of potential with pH indicates that approximately 2 H+ are transfe...
متن کاملThe binding of ferric iron by ferritin.
Equilibrium-dialysis experiments with 59Fe-labelled Fe(III) chelate solutions show that ferritin is capable of binding a limited number of Fe(III) atoms. Some of this Fe(III) is readily removed, but up to about 200 Fe(III) atoms/molecule remain bound after extensive washing. Some exchange of labelled Fe(III) with endogenous unlabelled ferritin Fe occurs during prolonged dialysis against 59Fe(II...
متن کاملMOSSBAUER SPECIROSCOPY OF Fe 2+ BINDING TO APO AND HOLO MAMMALIAN FERRITIN
The anaerobic binding of Fe 2+ to apo and holo Mammalian ferritin has been studied in the pH range from 6.0 to 10.0. Mossbauer spectroscopy of samples in which the added Fe 2+ is enriched in Fe-57 shows that the Fe 2+ ions bind to the ferritin core and exchange electrons with Fe 3+ ions in the core.
متن کاملPermeation of Fe2+ ions through three-fold pores of the human H-chain ferritin
Ferritin is a spherical protein that regulates the concentration of oxygen atom free radicals by keeping a sufficient amount of iron ions in the cytosol, thus reducing the possibility of oxidative stress that results in various life-threatening diseases such as diabetes, cancer, Alzheimer’s syndrome and others. [1,2,3] Ferritin conducts Fe ions from the cytoplasm, oxidizes them to Fe form, stor...
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ژورنال
عنوان ژورنال: Hyperfine Interactions
سال: 1987
ISSN: 0304-3843,1572-9540
DOI: 10.1007/bf02394111