Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. beta-Glucuronidase (EC 3.2.1.31) was purified from rabbit liver by a procedure involving autolysis, (NH(4))(2)SO(4) fractionation, chromatography on DEAE-cellulose and hydroxyapatite, gel filtration, sedimentation in a sucrose gradient, and isoelectric focusing. 2. Electron microscopy revealed ferritin as the major contaminant in later stages of purification and also showed aggregates of enzyme molecules. Particular attention was paid to the removal of ferritin. 3. The purified enzyme was homogeneous in polyacrylamide-gel electrophoresis both in non-dissociating conditions and in the presence of sodium dodecyl sulphate, and in Ouchterlony gel diffusion and immunoelectrophoresis against polyspecific antisera. 4. Sedimentation in sucrose gradients gave a molecular weight of 300000, whereas gel filtration indicated 440000. 5. Subunits of 75000 molecular weight were observed in gel electrophoresis in the presence of sodium dodecyl sulphate and in gel filtration in the presence of urea. 6. The K(m) value for p-nitrophenyl beta-d-glucuronide was 0.6mm, and the enzyme was extremely sensitive to lactone inhibitors. It was also inhibited by Hg(2+) ions. 7. Multiple forms were observed in the pure enzyme by isoelectric focusing, with pI values of 4.5-5.8. Subunits showed similar heterogeneity. The origin of the multiple forms was investigated in detail, and the possibility of artifact generation largely excluded. Some of the forms of lowest pI disappeared after neuraminidase digestion. The nature of the residual heterogeneity remains to be elucidated.
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PMID:Rabbit beta-glucuronidase. Purification and properties, and the existence of multiple forms. 421 18

1. Horse spleen ferritin and human liver ferritin were examined by gel electrofocusing under conditions that demonstrated equilibrium focusing. Both ferritins were resolved into multiple isoferritins. Both families of isoferritins were separable from one another. 2. Horse spleen ferritin was also resolved into five components by ion-exchange chromatography on DEAE-Sephadex A-50. Each of the major chromatographic fractions contained only a few of the isoferritins seen on gel electrofocusing. Each chromatographic fraction corresponded to different portions of the isoferritin profile. 3. These results indicate that the heterogeneity seen in many ferritins by gel electrofocusing represents structural heterogeneity in the ferritin population as isolated from the tissues.
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PMID:Heterogeneity in tissue ferritins displayed by gel electrofocusing. 447 67

Ferritin was extracted from human hepatocellular carcinoma tissue and purified using column chromatography, gradient gel electrophoresis and cadmium sulphate crystallization. DEAE cellulose chromatography showed a difference between hepatoma and normal liver ferritin, indicative of a more acidic isoferritin profile in the tumour. Column-purified and crystalline ferritin and that remaining in the mother-liquor after crystallization was subjected to isoelectric focusing. Hepatoma ferritin showed higher concentrations of acidic isoferritins than liver ferritin. This was most obvious with mother-liquor ferritin, as crystallization tended to select out more basic isoferritins. Subunit analysis of hepatoma and liver ferritin showed a higher proportion of heavy subunits in the tumour ferritin, in keeping with the presence of acidic isoferritins. An antibody against hepatoma mother-liquor ferritin was raised in rabbits. However, hepatoma ferritin proved to be antigenically identical with normal liver ferritin, and we were thus unable to develop a specific radioimmunoassay for hepatoma ferritin.
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PMID:Isolation of ferritin from human hepatocellular carcinoma. 609 60

Chrysotile asbestos interacts with mucin-secreting cells of tracheal organ cultures, causing an increase in secretion of mucin into the culture medium. This response occurs in the absence of obvious morphologic damage to tracheal epithelial cells. We speculated that asbestos-induced hypersecretion was regulated by the interaction of fibers with specific carbohydrate residues on the cell surface. To test this hypothesis, lectins, i.e., proteins with a high affinity for mono- and oligosaccharides on the plasma membrane, were added to tissues 30 min before addition of chrysotile. Secretion of mucin into the medium was then determined over a 2-hr period by using incorporation of 3H-glucosamine. Blocking of alpha-D-mannose and alpha-D-glucose residues inhibited chrysotile-induced hypersecretion (p less than 0.05), whereas lectins blocking residues of alpha-D-N-acetylgalactosamine, beta-D-N-acetylglucosamine, alpha-L-fucose and sialic acids were ineffective. Preincubation of cultures with carboxypeptidase A or phospholipase A2, but not with neuraminidase, diminished mucin secretion caused by chrysotile. To determine if the positive surface charge of chrysotile was important in interaction with mucin cells, we examined comparatively the effects of various polycations (cationic ferritin, polylysine, DEAE-dextran) and chrysotile after leaching of fibers to remove Mg2+. Although use of polycations enhanced secretion of mucin, effects were not as striking as those observed with chrysotile. In contrast, leached chrysotile failed to elicit a hypersecretory response. These results suggest the interaction of a positively charged component (presumably Mg2+) of chrysotile with glycolipids and glycoproteins containing terminal residues of alpha-D-mannose or alpha-D-glucose.
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PMID:Studies using lectins to determine mineral interactions with cellular membranes. 631 63

The biochemical characteristics of human placental and hepatic ferritins were compared. By DEAE cellulose column chromatography, placental ferritin was found to contain more acidic isoferritins, while hepatic ferritin was richer in basic isoferritins. The electrofocusing patterns of subunits revealed that placental ferritin contained at least one unique subunit on the acidic side and might lack one subunit on the basic side as compared with hepatic ferritin. It is hypothesized that microheterogeneities, immunological as well as biochemical, existing between placental and hepatic ferritins cannot be explained merely in terms of different proportions of known acidic and basic subunits, but appear to have resulted from the existence of the unique acidic subunit of placental ferritin and possibly also a unique basic subunit of hepatic ferritin.
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PMID:Possibly unique subunit(s) of human ferritins responsible for tissue specificity. 661 46

Bloodstream trypomastigote and culture procyclic (insect midgut) forms of a cloned T. rhodesiense variant (WRAT at 1) were tested for agglutination with the lectins concanavalin A (Con A), phytohemagglutinin P (PP), soybean agglutinin (SBA), fucose binding protein (FBP), wheat germ agglutinin (WGA), and castor bean lectin (RCA). Fluorescence-microscopic localization of lectin binding to both formalin-fixed trypomastigotes and red cells was determined with fluorescein isothiocyanate (FITC)-conjugated Con A, SBA, FBP, WGA, RCA, PNA (peanut agglutinin), DBA (Dolichos bifloris), and UEA (Ulex europaeus) lectins. Electron microscopic localization of lectin binding sites on bloodstream trypomastigotes was accomplished by the Con A-horseradish peroxidase-diamino-benzidine (HRP-DAB) technique, and by a Con A-biotin/avidin-ferritin method. Trypomastigotes, isolated by centrifugation or filtration through DEAE-cellulose or thawed after cryopreservation, were agglutinated by the lectins Con A and PP with agglutination strength scored as Con A greater than PP. No agglutination was observed in control preparations or with the lectins WGA, FBA or SBA. Red cells were agglutinated by all the lectins tested. Formalin-fixed bloodstream trypomastigotes bound FITC-Con A and FITC-RCA but not FITC-WAG, -SBA, -PNA, -UEA or -DBA lectins. All FITC-labeled lectins bound to red cells. Con A receptors, visualized by Con A-HRP-DAB and Con A-biotin/avidin-ferritin techniques, were distributed uniformly on T. rhodesiense bloodstream forms. No lectin receptors were visualized on control preparations. Culture procyclics lacked a cell surface coat and were agglutinated by Con A and WGA but not RCA, SBA, PP and FBP. Procyclics were not agglutinated by lectins in the presence of competing sugar at 0.25 M.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Trypanosoma rhodesiense bloodstream trypomastigote and culture procyclic cell surface carbohydrates. 668 36

We describe a method for the purification of normal human liver ferritin by ultrafiltration, gel filtration on Sephacryl S-300, and affinity chromatography on DEAE-Affi Gel Blue. The purity of the ferritin obtained was verified by immunoelectrophoresis, Ouchterlony immuno-diffusion, polyacrylamide gel electrophoresis, and electrofocusing. This rapid method yields 32% of the original ferritin.
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PMID:A three step purification procedure for human liver ferritin. 679 95

Anti 5-methyl-cytidine antibodies might be useful agents for the detection and localization of 5-methyl-cytidine of nucleic acids, but only if the antibodies recognize this nucleoside with sufficient specificity. A conjugate containing 18 moles of 5-methyl-cytidine per mole of BSA was prepared and antibodies directed against this nucleoside hapten were produced by immunization of rabbits (as determined by gel diffusion in agar containing excessive amounts of the carrier). A slight crossreaction of cytidine-BSA was eliminated by adsorption on the cross-reacting antigen. Further purification of the antibodies was effected by chromatography on DEAE-Sephadex A-50 and a method for the rapid quantitation of the antibodies showed that 12.7% of the IgG protein are monospecific against 5-methyl-cytidine-BSA. Hydrolysis of antibodies with insolubilized papain produced monovalent Fab fragments which were identified by SDS-Disk-electrophoresis. A two stage method for cross linking the immunoproteins to ferritin by glutaraldehyde was used. The isolation of immunoferritin conjugates by Bio-Gel A 1.5 m column chromatography is described. The identification of the effluents was made by glycerin density gradient ultracentrifugation. The results were visualized by electron microscopy after the treatment of immunoferritin conjugates with (methylated and unmethylated) denaturated DNA, fractionation on the glycerine density gradient, and the spreading by a modification of drop technique.
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PMID:Monospecific antibody against 5-methyl-cytidine for the structural analysis of nucleic acids. 711 47

When Chang liver cells are grown in an iron-rich medium for up to 20 weeks, iron loading up to 50 times the normal cellular iron content may be obtained, although ferritin increases only to about 10 times normal. Ferritin has been isolated from such cells, and the isoferritin pattern found on elution from DEAE-Sephadex A-50 by increasing chloride concentrations has been used as a basis for studying changes in the properties of ferritin under conditions of cellular loading. A consistent shift of peak ferritin-elution position to higher chloride concentrations (lower pI) occurs when cells are loaded with ferric nitrilotriacetate for increasing lengths of time. A change in immunoreactivity also takes place on loading, the ratio of ferritin reacting with heart and spleen ferritin antibodies increasing at any particular value of pI. Cells were pulse-labelled with [59Fe]ferric nitrilotriacetate and [3H]leucine followed by non-radioactive iron in the same form. During the 72 h after the synthesis of new protein and its incorporation of iron, there is a slight acid shift in its isoelectric point. This effect is seen in both normal and loaded cells, with the whole spectrum being shifted towards lower pI in the loaded state. These findings suggest that the shift to more acidic ferritins on iron loading and the associated changes in antigenicity may be unrelated to subunit composition.
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PMID:Changes in the characteristics and distribution of ferritin in iron-loaded cell cultures. 730 37

It has been demonstrated that a cytochrome b-containing ferritin is present in Azotobacter vinelandii. After DEAE cellulose chromatography and purification fractional precipitation by 50% of the saturated ammonium sulfate of the extract prepared from A. vinelandii cells, a hexagonal crystalline preparation is obtained. The protein contains 4--6% of nonheme iron. The protein molecule is made up of an electron dense iron core with a diameter of 70A and a protein shell with a diameter of 120A. The Fe core can be removed from the shell by the treatment with chelating and reducing agents. Electron micrographs and absorption spectra reveal that the protein shells are very similar before and after the removal of the core. The electrophoretic mobility and immunological properties of the Fe-free protein against the antibody of ferritin are very similar to those of the protein before the removal of the iron. From the above characteristics, it can be inferred that the protein belongs to ferritin. The protein part contains protoheme as prosthetic group and so it belongs to cytochrome b. Hence, the protein prepared from A. vinelandii is a kind of cytochrome b-containing ferritins. The possible role of the ferritin in biological nitrogen fixation is discussed in this paper.
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PMID:Presence of a cytochrome b-containing ferritin in Azotobacter vinelandii. 744 25


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