Results 251 to 260 of about 194,437 (305)
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Clinica Chimica Acta, 2005
Iron, an essential element for many important cellular functions in all living organisms, can catalyze the formation of potentially toxic free radicals. Excessive iron is sequestered by ferritin in a nontoxic and readily available form in a cell.
Sun-Ah, You, Qing, Wang
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Iron, an essential element for many important cellular functions in all living organisms, can catalyze the formation of potentially toxic free radicals. Excessive iron is sequestered by ferritin in a nontoxic and readily available form in a cell.
Sun-Ah, You, Qing, Wang
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The Lancet, 1973
FERRITIN is the major iron storage protein in the body. Although it is found in all tissues there is little quantitative information about its distribution.
G M, Addison +3 more
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FERRITIN is the major iron storage protein in the body. Although it is found in all tissues there is little quantitative information about its distribution.
G M, Addison +3 more
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The International Journal of Biochemistry & Cell Biology, 2004
A novel ferritin type specifically targeted to mitochondria has been recently found in human and mouse. It is structurally and functionally similar to the cytosolic ferritins, well-characterized molecules found in most living systems which are designed to store and detoxify cellular iron.
LEVI S, AROSIO, Paolo
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A novel ferritin type specifically targeted to mitochondria has been recently found in human and mouse. It is structurally and functionally similar to the cytosolic ferritins, well-characterized molecules found in most living systems which are designed to store and detoxify cellular iron.
LEVI S, AROSIO, Paolo
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Nature, 1968
ELECTROPHORETIC studies of ferritins—iron containing proteins—from horse, man and HeLa cells have already been recorded1,2. This communication describes the electrophoretic patterns of a plant ferritin known as phytoferritin3 and of ferritins from pig, ox and guinea-pig, compared with human and horse ferritin.
I, Zamiri, J, Mason
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ELECTROPHORETIC studies of ferritins—iron containing proteins—from horse, man and HeLa cells have already been recorded1,2. This communication describes the electrophoretic patterns of a plant ferritin known as phytoferritin3 and of ferritins from pig, ox and guinea-pig, compared with human and horse ferritin.
I, Zamiri, J, Mason
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Science, 1942
Publisher Summary In 1894, Schmiedeberg prepared an iron-containing protein from pig's liver, containing about 7% iron. This poorly defined compound was obtained in a denatured condition. The first decisive step was made with Laufberger's discovery of a readily crystallizable protein, containing as much as about 20% of iron, in the ferric state.
S, Granick, L, Michaelis
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Publisher Summary In 1894, Schmiedeberg prepared an iron-containing protein from pig's liver, containing about 7% iron. This poorly defined compound was obtained in a denatured condition. The first decisive step was made with Laufberger's discovery of a readily crystallizable protein, containing as much as about 20% of iron, in the ferric state.
S, Granick, L, Michaelis
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Blood Reviews, 1990
The iron storage protein ferritin is found in all cells of the body as multiple isoferritins composed of 24 sub units of two types. The structure is well understood from increasingly detailed analysis by X-ray crystallography. Genes for the principal subunits (called H and L) have been cloned and are located on chromosomes 11q and 19q respectively. The
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The iron storage protein ferritin is found in all cells of the body as multiple isoferritins composed of 24 sub units of two types. The structure is well understood from increasingly detailed analysis by X-ray crystallography. Genes for the principal subunits (called H and L) have been cloned and are located on chromosomes 11q and 19q respectively. The
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Archives of Biochemistry and Biophysics, 1989
Apoferritins prepared from horse spleen and heart and rat heart and liver were dissociated by treatment with acetic acid (pH 1.3-3.0). Sedimentation velocity studies showed that apoferritins of spleen and liver (16-17 S) and heart (18-19 S) dissociated into material sedimenting near 3.2 S.
M C, Linder +4 more
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Apoferritins prepared from horse spleen and heart and rat heart and liver were dissociated by treatment with acetic acid (pH 1.3-3.0). Sedimentation velocity studies showed that apoferritins of spleen and liver (16-17 S) and heart (18-19 S) dissociated into material sedimenting near 3.2 S.
M C, Linder +4 more
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Ferritin drug carrier (FDC) for tumor targeting therapy
Journal of Controlled Release, 2019Ferritin is an iron storage protein that plays a key role in iron homeostasis and anti-oxidation of cells. Due to its unique architecture of 24 self-assembling subunits and hollow cavity capable of encapsulating drugs, and an outer surface that can be ...
Jiuyang He, Kelong Fan, Xiyun Yan
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Interaction of ferritin with serum: implications for ferritin turnover
Clinica Chimica Acta, 1984An interaction between human and rabbit ferritins and serum was demonstrated by a coated tube binding assay, a shift in molecular size on gel filtration and by precipitation of complexes with 3.5% polyethylene glycol 6000. With polyethylene glycol and labelled ferritins, complex formation was inhibited by heating sera to 56 degrees C for 30 min and by ...
A M, Covell, A, Jacobs, M, Worwood
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Reactivity of ferritin and the structure of ferritin-derived ferrihydrite
Biochimica et Biophysica Acta (BBA) - General Subjects, 2010In nature or in the laboratory, the roughly spherical interior of the ferritin protein is well suited for the formation and storage of a variety of nanosized metal oxy-hydroxide compounds which hold promise for a range of applications. However, the linkages between ferritin reactivity and the structure and physicochemical properties of the nanoparticle
F Marc, Michel +5 more
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