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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The transfer of iron between horse spleen [55Fe]ferritin and human apotransferrin or [59Fe]transferrin in homogeneous solution was investigated. Transfer between the two proteins in the presence of citrate, ATP, or ascorbate occurs in both direction, but the net flow is always from ferritin to transferrin. Ferritin which is ca. 1/3 to 1/2 saturated with iron appears to be most reactive. Chemically prepared apoferritin does not accept iron from diferric transferrin. Citrate-mediated transfer of iron from ferritin to apotransferrin is first order with respect to ferritin, zero order with respect to transferrin, and has a complex dependence upon citrate concentration. Direct transfer of iron from native or reconstituted ferritin to apotransferrin in the absence of any identifiable mediating agent was observed to occur at about half the rate attained in the presence of 1 mM citrate. No transfer of iron between the two proteins occurs across a dialysis membrane in the absence of a mediating agent. No binding of transferrin and ferritin to each other was demonstrable. One possible explanation for these observations is that iron from the core of ferritin is in equilibrium with iron near the outer surface of the protein, where the metal would be available to transferrin.
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PMID:Iron exchange between ferritin and transferrin in vitro. 69 86

The inter-relationships between serum ferritin, hemoglobin, serum iron and total body iron stores were studied in 20 patients with chronic renal failure treated conservatively and in 20 patients on regular hemodialysis. There was no relationship between serum iron or transferrin and bone marrow iron deposits, but serum ferritin concentration was a good indicator of increased marrow iron stores. All patients with serum ferritin levels above 300 microgram/l had increased iron stores. Serum ferritin assay is a useful non-invasive technique for detecting iron overload in uremic and hemodialyzed patients.
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PMID:Serum ferritin concentration: a reliable guide to iron overload in uremic and hemodialyzed patients. 69 5

We followed up 238 infants on 7 occasions during their first year of life. The diets of the infants were systematically either supplemented or not supplemented with iron. Developmental changes in serum ferritin were determined from a group with adequate intake of iron and without evidence of iron deficiency by three laboratory criteria: hemoglobin, mean corpuscular volume and transferrin saturation. The data indicate that the average level of serum ferritin correlates well with iron nutrition within groups of infants since the developmental changes are in accordance with the known changes in storage iron, the level of serum ferritin correlates with iron intake, and low ferritin levels are associated with lower transferrin saturation. The usefulness of serum ferritin as the sole criterion of iron deficiency in individual infants is limited, suggesting the use of more than one indicator to refine the diagnosis of iron deficiency without anemia.
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PMID:Serum ferritin in assessment of iron nutrition in healthy infants. 71 74

Serum ferritin, transferrin, iron and haptoglobin have been investigated in a longitudinal study in 18 patients hospitalized for various acute infections. Within a couple of days after the onset of an infection, a rise in serum ferritin was seen, the magnitude of which was not dependent on the type of infection (bacterial or viral). The serum ferritin level remained elevated for several weeks in some patients, and 7 out of the 18 patients still had abnormally high values 5 weeks after the onset of illness. The mean curves for serum ferritin and the acute phase reactant haptoglobin were parallel. Possible mechanisms causing the elevation in serum ferritin are discussed.
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PMID:Serum ferritin during infection. A longitudinal study. 72 31

Iron uptake by Chang liver cells in culture is about thirty times as great when ferric nitriloacetate is used as a donor as when iron-transferrin is used. Iron uptake from ferric citrate is no greater than from iron-transferrin. Most of the intracellular iron derived from transferrin is found in the supernatant after 20 000 x g centrifugation of the cell homogenate for 40 min: about half of this is in the form of ferritin. Iron derived from ferric nitriloacetate is found largely in the membranous pellet after centrifugation and very little of this is in the form of ferritin. Iron incorporated in cytosol ferritin is easily available for chelation by desferrioxamine and this process is facilitated by ascorbic acid. Membrane-bound iron is less available for chelation. This tissue culture model forms a convenient basis for the study of iron overlead and iron chelation.
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PMID:Iron uptake by Chang cells from transferrin, nitriloacetate and citrate complexes: the effects of iron-loading and chelation with desferrioxamine. 72 60

The efficacy of measuring the transferrin saturation and the serum ferritin concentration to detect iron deficiency was determined under routine conditions in a general hospital. The tests were performed on 100 adult patients who consecutively underwent bone marrow aspiration for the appraisal of a wide range of clinical conditions. The absence of stainable reticuloendothelial iron in smears of the aspirate was used as the benchmark of iron deficiency. Of the 86 patients who were anemic 19 lacked hemosiderin in the bone marrow. The percentage of patients with iron deficiency who were correctly classified by the tests (i.e., the tests' sensitivity) was 84% for the transferrin saturation and 79% for the serum ferritin concentration, and the percentage of patients free of iron deficiency who were correctly classified by the tests (i.e., the tests' specificity) was 63% and 96% respectively. The predictive value of an abnormal (positive) result for the detection of iron deficiency was 39% for the transferrin saturation and 83% for the serum ferritin concentration, whereas the predictive value of a normal or high (negative) result for the exclusion of iron deficiency was 93% and 94% respectively. Measurement of the serum ferritin concentration was superior to measurement of the transferrin saturation only in its specificity. The former is of particular value in clinical settings where the prevalence of iron deficiency is low and conditions that increase the serum ferritin concentration out of proportion to the size of the body iron stores are infrequent.
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PMID:Usefulness of the serum ferritin concentration in the detection of iron deficiency in a general hospital. 73 38

The diagnostic value of serum ferritin measurements in discriminating iron-deficiency anemia from thalassemia trait has been studied. In contrast to serum iron, percent transferrin saturation and total iron-binding capacity, where a high degree of overlap existed between the two groups, a clear-cut difference in serum ferritin levels was found between iron deficiency and thalassemia trait. The best separation of iron deficiency, thalassemia and normal controls was given by the combination of mean corpuscular volume and serum ferritin. Although definitive diagnosis of beta-thalassemia trait requires the demonstration of abnormal Hb A2 levels or beta-chain synthesis, serum ferritin is a useful screening test for the initial diagnosis of thalassemia trait. Because of the very small amounts of serum required for the measurement of ferritin, it is particularly suitable for surveying populations with a high prevalence of hypochromic-microcytic anemias.
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PMID:Serum ferritin in beta-thalassemia trait. 75 May 37

The protoporphyrinemia of iron deficiency is well recognized. Clinically, information on the protoporphyrin/heme molar ratio in whole blood offers certain advantages over protoporphyrin measurement alone. A procedure for determining this ratio is reported. Protoporphyrin is extracted, solubilized, and measured fluorometrically. Heme (as hemin chloride) is precipitated with the blood proteins, the precipitate is dissolved in an alkaline/pyridine solvent, and the resulting bispyridine ferriprotoporphyrin is measured spectrophotometrically. The molar ratio of these two metabolites correlates well with values for plasma ferritin, plasma iron, transferrin saturation, hemoglobin, and hematocrit. In some cases the ratio increases detectably while the other variables, especially hematocrit and hemoglobin, remain normal. Evidently it is a more sensitive index to iron status. For healthy men and women, the mean ratio is 16.0 (SD, 5.3). The mean + 3 SD, or a ratio of 32, is distinctly abnormal, as shown by a confirmatory test. We validated the test by surveying routine blood specimens obtained from several population groups.
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PMID:Erythrocyte protoporphyrin/heme ratio in the assessment of iron status. 76 86

After in vivo infusion, radio-active indium is fixed by liver and bone marrow, but more slowly and less completely than iron. It does not incorporate to haem. It is found as labelled ferritin in the liver, after the fifth day. In the bone marrow, indium is almost exclusively found as labelled transferrin; several arguments suggest the intra-cellular site of the labelled protein. Using indium may enable a better knowledge of the intermediary iron pools.
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PMID:[Study of proteins binding radioactive indium in vivo]. 81 62

The detailed reversible binding isotherms of sodium dodecyl sulfate (NaDodSO4) with 13 different initially native proteins are reported; the data were obtained at 20 degrees C and pH 7.1, ionic strength 0.033, with amounts bound with some proteins up to 1.1 g per g of protein. Although the isotherms of some of the proteins do not vary widely, extreme variations between certain classes are found. Thus, for example, hemoglobin and myoglobin both have high affinities and high binding capacities, while gamma-globulin, apoferritin, and transferrin have low initial affinities, and change drastically at higher concentrations. The protein-NaDodSO4 complexes solubilize the water-insoluble dye dimethylaminoazobenzene (DMAB) as effectively as micelles of pure NaDodSO4 when only small amounts (0.2 to 0.5 g/g of NaDodSO4) are bound. In most cases this effectiveness falls progressively as larger amounts are bound, and may even cease altogether at limits characteristic of the individual protein. With some of the latter, a second region of renewed solubilization occurs when substantially higher amounts of NaDodSO4 are present. In all cases, solubilization by ordinary micelles in normal amount occurs when the free NaDodSO4 concentration exceeds the critical micelle concentration, but the binding of NPADodSO4 to the protein also increases, in competition with formation of micelles. With some, but not all proteins the NaDodSO4 bound at concentrations above the cmc also solubilizes DMAB. In such cases the solubilizations by the protein-NaDodSO4 complexes and by the simple micelles are additive. The significance of the differences in binding and solubilizing encountered among these proteins is discussed in terms of surface structure, cooperativity of binding, and protein composition. No certain correlations with content of most amino acids, subunit structure, solubility, and hydrophobicity have been found, but there is a weak inverse dependence of solubilizing effectiveness on molecular size and indications of a strong dependence on content of cationic groups.
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PMID:Differences in the solubilizing effectiveness of the sodium dodecyl sulfate complexes of various proteins. 83 11


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