Kinetics of iron release from pig spleen ferritin with bare platinum electrode reduction

Huang, Heqing; Lin, Qi; Wang, T.L.

doi:10.1016/s0301-4622(02)00007-8

Cited by 21 publications

(12 citation statements)

References 31 publications

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“…Electronic tunnels consisted of some amino acid residues and were responsible for electronic transfer, storage and release of irons[63, 64]. Analysis of anion loading into ferritin after the iron core was established that allowed the anions to deposit on the mineral core.…”

Section: Discussionmentioning

confidence: 99%

Preparation and Representation of Recombinant Mn-Ferritin Flower-Like Spherical Aggregates from Marine Invertebrates

et al. 2015

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Ferritin has important functions in the transition and storage of toxic metal ions, but its regulation and function in many invertebrate species are still largely unknown. In our previous work, the cDNA sequence of Sinonovacula constricta, Apostichopus japonicas and Acaudina leucoprocta were constructed and efficiently expressed in E. Coli BL21 under IPTG induction. In this follow-up study, the recombinant ferritins were exposed to heavy metal manganese. The manganese concentration levels in three recombinant ferritins were greater than horse spleen ferritin (HSF). Compared with HSF, the amount of manganese enrichment in the three recombinant ferritins was 1.75-fold, 3.25-fold and 2.42-fold increases in ScFER, AjFER, and AlFER, respectively. After phosphate stimulation, the concentration of manganese increased and was higher than the ordinary dialysis control groups. The ScFER was four times its baseline value. The AjFER and AlFER were 1.4- and 8-fold higher, respectively. The AlFER sample stimulated by phosphate was 22-fold that of HSF. The morphologies of the resulting Mn-Ferritin from different marine invertebrates were characterized with scanning electron microscopy. Surface morphologies were lamella flower-like and are consistent with changes in surface morphologies of the standard Mn-HSF. Invertebrate recombinant ferritin and HSF both can uptake manganese. We found that the structure of A. leucoproctarecombinant Mn-Ferritin aggregate changed over time. The surface formed lamella flower-like aggregate, but gradually merged to create a relatively uniform plate-like phase of aggregate spherically and fused without clear boundaries.

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Section: Discussionmentioning

confidence: 99%

Preparation and Representation of Recombinant Mn-Ferritin Flower-Like Spherical Aggregates from Marine Invertebrates

et al. 2015

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“…The sheep liver/heart ferritins were isolated according to the method for the isolation of pig spleen ferritin [22] with a little modification. After homogenization and heat treatment, the liver homogenate was centrifuged at 2500×g for 15 min.…”

Section: Isolation and Purification Of Ferritinmentioning

confidence: 99%

Direct evidence for non-specific peroxidase activity of ‘‘ferritin–heme” complex: possible role in the development of neurodegenerative diseases

et al. 2014

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“…2B, curve b). Ferritin is a large Fe storage protein (Theil et al, 1983;Ford et al, 1984), and Fe(II) ions can be released from ferritin by AA (Ahmad et al, 2000;Roginsky et al, 1997;Huang et al, 2002). The released free Fe(II) ions can react with hydrogen peroxide and form hydroxyl radical, which may induce DNA damage (Ahmad et al, 2000).…”

Section: Detection Of Dna Damage Induced By Ferritin/aa/h 2 O 2 Systemmentioning

confidence: 99%

“…The maximal of 4500 iron atoms as a hydrous ferric oxide can be stored in each ferritin molecule (Harrison et al, 1974;Boyer and McCleary, 1987). Numerous biologically significant reducing agents such as ascorbic acid (AA) can release iron from ferritin through the reduction of tightly bound Fe(III) to more mobile Fe(II) ions (Boyer and McCleary, 1987;Ahmad et al, 2000;Roginsky et al, 1997;Huang et al, 2002). The released free iron may catalyze deleterious reactions and result in increased generation of ROSs in cells, which in turn can damage cellular biomacromolecules such as DNA, proteins and lipids (Ahmad et al, 2000(Ahmad et al, , 1995.…”

Section: Introductionmentioning

confidence: 99%

Electrochemical detection of natural DNA damage induced by ferritin/ascobic acid/H2O2 system and amplification of DNA damage by endonuclease Fpg

Liu

2009

Biosensors and Bioelectronics

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Kinetics of iron release from pig spleen ferritin with bare platinum electrode reduction

Cited by 21 publications

References 31 publications

Preparation and Representation of Recombinant Mn-Ferritin Flower-Like Spherical Aggregates from Marine Invertebrates

Preparation and Representation of Recombinant Mn-Ferritin Flower-Like Spherical Aggregates from Marine Invertebrates

Direct evidence for non-specific peroxidase activity of ‘‘ferritin–heme” complex: possible role in the development of neurodegenerative diseases

Electrochemical detection of natural DNA damage induced by ferritin/ascobic acid/H2O2 system and amplification of DNA damage by endonuclease Fpg

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