Ferritin: Iron incorporation and iron release

Niederer, Werner

doi:10.1007/bf01895596

Cited by 78 publications

(40 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have shown (Macara et al, 1972(Macara et al, , 1973, as have others (Niederer, 1970;Bryce & Crichton, 1973b), that horse spleen apoferritin catalyses the oxidation of Fe(II) to Fe(III), retaining the latter as hydrous ferric oxide to give ferritin. We wished to discover whether individual 'isoferritins' (ferritins from different tissues or fractions of different isoelectric point from the same tissue) showed any functional differences as judged by their ability to oxidize and accumulate iron in vitro and to observe the effects of both removal and addi-tion of iron on their focusing patterns.…”

supporting

confidence: 63%

Heterogeneity in horse ferritins. A comparative study of surface charge, iron content and kinetics of iron uptake

Russell¹,

Harrison²

1978

Biochemical Journal

View full text Add to dashboard Cite

Horse ferritins from different organs show heterogeneity on electrofocusing in Ampholine gradients. Both ferritin and apoferritin from liver and spleen could be fractionated with respect to surface charge by serial precipitation with (NHI4)2SO4. In the ferritin fractions, increasing iron content parallels increasing isoelectric point. After removal of their iron those fractions which originally contained most iron accumulated added iron at the fastest rates. When unfractionated ferritins from different organs were compared the average isoelectric point increased in order spleen< liver< kidney< heart. The order of initial rates of iron uptake by the apoferritins was spleen> kidney> heart and initial average iron contents also followed this order. The relatively low rates of iron accumulation by ironpoor molecules may have been due to structural alteration, to degradation, to activation of the iron-rich molecules or to other factors.

show abstract

supporting

confidence: 63%

Heterogeneity in horse ferritins. A comparative study of surface charge, iron content and kinetics of iron uptake

Russell¹,

Harrison²

1978

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…Neiderer [279] advanced the hypothesis that Fe(I1) ions could penetrate the protein shell of the apoferritin molecule where their oxidation would be catalysed by the protein: the nascent ferric ions would form an intramolecular precipitate of FeO . OH which would soon be too big to escape.…”

Section: Iron Deposition In Ferritinmentioning

confidence: 99%

Iron transport and storage

Crichton

Charloteaux-Wauters

1987

European Journal of Biochemistry

489

246

View full text Add to dashboard Cite

“…In vitro ferritin reconstitution can be achieved by the addition of Fe(I1) to apoferritin in the presence of an oxidant [2,3]. Apoferritin facilitates ferrihydrite formation by providing sites at which Fe(I1) oxidation is accelerated and those at which the iron-core mineral is nucleated [3] which may or may not be the same.…”

Section: Introductionmentioning

confidence: 99%