A procedure for the purification of ferritin from human liver by heating a methanol-treated homogenate

Cham, Bill E.; Roeser, H. P.; Nikles, A.; Ridgway, Kathleen M.

doi:10.1016/0003-2697(85)90220-9

Cited by 33 publications

(18 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have added rats to our study as a mammalian reference species. Comparisons of the present results with earlier studies provide corresponding values for the yield of ferritin protein in rat or mouse liver and mucosa (Cham et al ., 1985;Ehtechami et al ., 1989;Gérard et al ., 1996). In birds and some other species, only liver ferritin has been studied previously with a much lower yield than ours (10-fold to 100-fold) (Gonzalez del Barrio & Martin Mateo, 1983;Suryakala & Deshpande, 1999).…”

Section: Discussionsupporting

confidence: 81%

See 1 more Smart Citation

Partial purification and characterization of ferritin from the liver and intestinal mucosa of chickens, turtledoves and mynahs

et al. 2005

View full text Add to dashboard Cite

Ferritin is the iron-storage protein responsible for sequestering excess iron, to be stored in a safe way in the liver or to be shed with the intestinal epithelial cells. The properties of ferritin in iron-overload-susceptible birds have not been elucidated. Furthermore, there is only scarce information on mucosal ferritin, with no information at all in avian species. Here we have studied the liver and proximal intestine ferritins of iron-overload-susceptible (Indian hill mynahs, common mynahs) and non-susceptible (turtledoves, chicken) bird species. A brief purification process preceded native polyacrylamide gel electrophoresis and staining the gels for protein and iron. Protein amounts and iron-binding characteristics of ferritin were measured and ferritin saturation levels were calculated. Although ferritin protein amounts did not differ significantly, liver and mucosal ferritins of sensitive bird species incorporated much more iron, leading to high saturation levels. Significantly higher ferritin iron content and saturation were observed in the liver of both mynah species and in the intestinal ferritin of Indian hill mynahs when compared with the non-susceptible species. Ferritin appears not to play a major role in the regulation of iron absorption, implicating other phases in iron transport to be more important in the onset and process of iron overload in birds.

show abstract

Section: Discussionsupporting

confidence: 81%

“…This may be due to the purification process. The high yield we have obtained may be due to the lower loss of protein achieved by our procedure since multiple steps used in the isolation and purification of ferritin cause high losses of the protein (Frenkel et al ., 1983;Cham et al ., 1985Cham et al ., , 1986.…”

Section: Discussionmentioning

confidence: 93%

Partial purification and characterization of ferritin from the liver and intestinal mucosa of chickens, turtledoves and mynahs

et al. 2005

View full text Add to dashboard Cite

show abstract

“…Firstly, froin the iron-loaded tissues of treated (venesected; n = 2) and untreated PH (n = 1) and treated (chelated; n = 2) SH patients: secondly, from the spleen of horse (n = 1) in which iron loading occurs naturally; thirdly froin the livers of rats, which were either iron-loaded for four weeks with the ferrocene compound, iron loaded then given intraperitoneal injection of 10 mg/kg desferrioxamine three times each week, or Cham et al (1985). The detcction limit for Cu, Cd, Ra, Pb and Co was 1 nmol/mol Fe, and for Na, K, Mg, Ca, P, Zn, Li, Be, Cr, Mo, Mn, Co, Ni and Pb was 0.4 pmol/mol Fe.…”

Section: Methodsmentioning

confidence: 99%

“…For haemosiderin preparation, the livers from the three rats in each group were combined. Ferritin was extracted from the tissue supernatant by the method of Cham et al (1985). The iron cores in each haemosiderin were characterised by Mossbauer spectroscopy, as previously described .…”

Section: Methodsmentioning

confidence: 99%

Chemical and structural characterisation of iron cores of haemosiderins isolated from different sources

Ward

Dickson

Florence

et al. 1992

European Journal of Biochemistry

View full text Add to dashboard Cite

The elemental content of the iron cores of haemosiderins isolated from animal and human tissues has been determined to ascertain whether changes in composition are correlated with structural differences previously identified in these mineralisation products. Significant differences were observed in the elemental composition of haemosiderins isolated from patients subjected to desferrioxamine‐chelation therapy compared to patients who had been venesected. The P/Fe molar ratio was considerably higher in haemosiderin isolated from treated primary haemochromatosis (0.83), compared to untreated primary haemochromatosis (0.10) and treated secondary haemochromatosis (0.25), and this could account for the amorphous nature of these iron cores. The levels of M/Fe (M = Ca, Cu, Zn) were reduced in the haemosiderins derived from treated secondary haemochromatosis patients, possibly due to the chelation of these ions by desferrioxamine therapy. In an experimentally iron‐loaded rat, receiving either desferrioxamine or 1,2‐diethyl‐3‐hydroxypyrid‐4‐one, selective decreases in these three elements were also observed after two weeks of desferrioxamine therapy. Such changes may be important determinants in the modification of biomineralisation of the iron cores.

show abstract

“…Ferritin was partially purified from plasma samples according to the method of Cham et al [1985], and then it was detected by immunoblotting. In brief, mice were anesthetized via Halothane (Halocarbon Laboratories, River Edge, N.J., USA) inhalation and blood was collected into heparinized tubes that were prepared by drying 10 Ìl of heparin at 1,000 units/ml (Elkin-Sinn, Inc, Cherry Hill, N.J., USA) in plastic centrifuge tubes.…”

Section: Plasma Ferritin Analysismentioning

confidence: 99%

Apoferritin Attenuates Experimental Allergic Encephalomyelitis in SJL Mice

Levine

Maiti²,

Emerson³

et al. 2002

Dev Neurosci

View full text Add to dashboard Cite

Ferritin has been shown to attenuate iron-catalyzed oxidative damage in several experimental conditions. Since oxidative damage has been implicated in the pathogenesis of multiple sclerosis (MS) and experimental allergic encephalomyelitis (EAE), an animal model of MS, we tested the hypothesis that ferritin would act to attenuate disease. The experimental design was to increase plasma ferritin levels during the active stage of EAE by giving systemic injections of apoferritin and then compare disease activity between these mice and EAE mice administered vehicle. Additional mice received systemic injections of iron, which induces ferritin synthesis, in order to test the effects of exogenous iron on the disease course. Although plasma levels of ferritin were found to be elevated in both apoferritin and iron-injected EAE mice, only apoferritin treatment resulted in a reduction in disease activity compared to EAE mice given vehicle. The suppressive effects of apoferritin administration suggest that the increase in endogenous ferritin levels that have been previously observed in the cerebrospinal fluid of chronic progressive MS patients with active disease might be functioning to limit the severity and spread of tissue damage.

show abstract

A procedure for the purification of ferritin from human liver by heating a methanol-treated homogenate

Cited by 33 publications

References 7 publications

Partial purification and characterization of ferritin from the liver and intestinal mucosa of chickens, turtledoves and mynahs

Partial purification and characterization of ferritin from the liver and intestinal mucosa of chickens, turtledoves and mynahs

Chemical and structural characterisation of iron cores of haemosiderins isolated from different sources

Apoferritin Attenuates Experimental Allergic Encephalomyelitis in SJL Mice

Contact Info

Product

Resources

About