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

To learn more about pathological iron storage in the liver, two sorts of lysosomes were isolated from rat livers in Percoll - sucrose or sucrose gradients: siderosomes (= iron-loaded terminal lysosomes) and light lysosomes (secondary and terminal). Such cell fractions were obtained from acutely iron-loaded and control rat livers. After lysis with Triton X-100 the preparations were assayed for proteolytic activity against rat liver ferritin (RLF) and denatured bovine hemoglobin (DBH), for buffer-soluble ferritin protein content, total protein and non-heme iron. At pH 3.6 both fractions displayed considerable proteolytic activity (cathepsin D activity) against DBH and endogenous proteins but little activity against RLF. By contrast, proteolytic activity against RLF was maximal at the highest pH tested, 6.5, at which DBH was practically insusceptible. The behavior of proteolytic activity against ferritin at pH 6.5 makes it likely that a single enzyme was involved that acted by Michaelis-Menten kinetics. However, no more than 2.5% of endogenous ferritin protein in the organelles was buffer-soluble. 41 to 89 hours after an intramuscular dose of 50 mg Fe, given as iron dextran, the non-heme iron content of light lysosomes and siderosomes had increased markedly and the ratio of non-heme Fe to buffer-soluble ferritin protein also became much elevated in the organelles; but the ratio of buffer-soluble ferritin to total protein did not rise significantly. The rise in organellar non-heme Fe exceeded iron saturation of rat liver ferritin and thus reflected conversion of ferritin to hemosiderin, which is buffer-insoluble.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Studies of iron overload. Lysosomal proteolysis of rat liver ferritin. 373 72

Yeast plasma membranes have been isolated from homogenized yeast cells, identified as pure plasma membrane vesicles which were used as antigens. By crossed immunoelectrophoresis with anti-membrane immunoglobulins, 17 discrete antigens have been detected in Triton X-100 extracts from plasma membranes. Three different immunoabsorption experiments were performed with : a) isolated membranes exposing the cytoplasmic surfaces (PS) and the external surfaces (ES), b) yeast protoplasts exposing only antigenic determinants on the ES, c) lysed protoplasts which had been saturated on the ES with antibodies prior to lysis. These absorption experiments demonstrated that seven of the antigens are expressed on the ES while eight immunogens expose antigenic determinants on the PS. Four of the principal immunoprecipitates are not affected by absorption with surface antigens whereas two of the antigens indicate transmembrane characteristics. Of these 17 immunoprecipitates four were shown by zymograms to possess enzymatic activities: ATPase (EC 3.6.1.3) and NADH-dehydrogenase (EC 1.8.99.3) (three separate components). Three of these enzymes are expressed on the PS, and one NADH-dehydrogenase exposes determinants on the ES of the protoplasts. The presence of antigens on the PS of the plasma membrane could also be demonstrated on micrographs by the indirect ferritin-antibody labeling technique followed by freeze-etching and shadowing of the membranes.
 ...
PMID:Immunochemical analysis of the plasma membrane from baker's yeast Saccharomyces cerevisiae. 616 18

This study systematically examined the characteristics of specific binding of adult diferric transferrin to its receptor using a Triton X-100 solubilized preparation from human placentas as the receptor source. The following information was obtained. The ionic strength for maximal binding is in the range of 0.1-0.3 M NaCl. The pH optimum for specific binding extends over the range, from pH 6.0-10.0. Specific binding of diferric transferrin is not affected by 2.5 approximately 50 mM CaCl2 or by 10 mM EDTA. Triton X-100 in the concentration range of 0.02-3.0% does not affect specific binding. Specific binding is saturated within 10 min at 25 or 37 degrees C in the presence of excess amounts of diferric transferrin. The binding is reversible and the dissociation of diferric transferrin from the transferrin receptor is complete within 40 min at 25 degrees C. Apotransferrin, both adult and fetal, showed less binding than the holotransferrin species by competitive binding assay in the presence of 10 mM EDTA independent of up to 20 mM CaCl2. A 1500-fold molar excess of adult and fetal apotransferrin is required to give 40% inhibition for 125I-labeled diferric transferrin binding. Since calcium ion is not a factor, and since apotransferrin has such high binding affinity for iron (Ka = 1 X 10(24], this experiment suggests that the EDTA was necessary to prevent conversion of apotransferrin to holotransferrin from available iron in the reaction system. The specificity of the transferrin receptor for transferrin was examined by competitive binding studies in which 125I-diferric transferrin binding was measured in the presence of a series of other proteins. The proteins tested in the competitive binding studies were classified into three groups; in the first group were human serum albumin and ovalbumin; in the second group were proteins containing iron ions, such as hemoglobin, hemoglobin-haptoglobin complex, heme-hemopexin complex, ferritin, and diferric lactoferrin; in the third group were the metal-binding serum proteins, ceruloplasmin and metallothionein. None of these proteins except ferritin showed inhibition of diferric transferrin binding to the receptor. The effect of ferritin was small since a 700- to 1500-fold molar excess of ferritin is required for 50% inhibition of binding of diferric transferrin to the receptor.
 ...
PMID:Characterization of transferrin binding and specificity of the placental transferrin receptor. 631 Nov 10

Bovine bone morphogenetic protein (bBMP) induces differentiation of mesenchymal-type cells into cartilage and bone. bBMP has an apparent Mr of 18,500 +/- 500 and represents less than 0.001% of the wet weight of bone tissue. A Mr 34,000 protein resembling osteonectin is separated by extraction with Triton X-100. A Mr 24,000 protein and about half of a Mr 22,000 protein are disassociated from bBMP by precipitation in 1.5 M guanidine hydrochloride. Aggregates of bBMP and a Mr 14,000 protein are insoluble in aqueous media; the bBMP becomes soluble when the Mr 14,000 protein is disassociated in 6 M urea and removed from the solution by ultrafiltration. Three separate molecular species with apparent Mrs 18,500, 17,500, and 17,000 are eluted at 0.10, 0.15, and 0.20 M phosphate ion concentrations, respectively, from a hydroxy-apatite column. The Mr 18,500 protein has the amino acid composition of acidic polylpeptide and includes four half-cystine residues; the pI is 4.9-5.1. The Mr 22,000 component is a chromoprotein resembling ferritin. The NH2-terminal amino acid sequence of the Mr 17,500 protein simulates histone H2B. The Mr 17,000 protein may possess calmodulin activity. Aggregates of the Mr 18,500 and other proteins induce formation of large deposits of bone; the Mr 18,500 protein alone is rapidly absorbed and induces formation of small deposits. None of the other proteins induces bone formation.
 ...
PMID:Purification of bovine bone morphogenetic protein by hydroxyapatite chromatography. 632 Jan 84

The subcellular location of the major malarial glycoprotein in erythrocytes infected with schizonts of Plasmodium falciparum has been studied by two methods. In the first, glycoproteins were labelled with [3H]glucosamine or [3H]isoleucine during in vitro culture. Trypsin treatment of intact infected erythrocytes caused no major qualitative or quantitative changes in [3H]glucosamine labelled glycoproteins or [3H]isoleucine labelled proteins separated by sodium dodecylsulfate polyacrylamide gel electrophoresis. However, in the presence of Triton X-100 the labelled glycoproteins and proteins were completely cleaved by trypsin. In the second method, two monoclonal antibodies which specifically immunoprecipitate the major 195 kDa glycoprotein failed to react on indirect immunofluorescence with intact non-fixed schizont-infected erythrocytes, but reacted strongly with saponin released schizonts indicating specificity for the surface of mature intracellular parasites. Immunoelectronmicroscopy using ferritin-conjugated secondary antibody confirmed the location of the epitope(s) recognized by these monoclonals on the surface of intracellular parasites. Ferritin particles were not associated with knob-bearing erythrocyte membranes. The results indicate that only a small proportion or none of the 195 kDa glycoprotein is on the surface of the infected erythrocyte and that the largest proportion is expressed on the surface of mature intraerythrocytic parasites.
 ...
PMID:Localization of the major Plasmodium falciparum glycoprotein on the surface of mature intraerythrocytic trophozoites and schizonts. 637 50

Because of the potential significance of external components of the obligate intracellular parasite Rickettsia rickettsii in host-parasite interactions, we have begun the first phase of a study to isolate and characterize surface antigens of this organism. An antiserum to a rickettsial surface component was obtained from rabbits inoculated with immune precipitates prepared by crossed immunoelectrophoresis of Triton X-100 extracts of R. rickettsii strain R. This antiserum (i) protected guinea pigs inoculated with 10,000 guinea pig 50% infectious doses of R. rickettsii against fever, (ii) prevented death of mice challenged with 2 50% lethal doses of R. rickettsii, and (iii) reacted in the microimmunofluorescence test with 9 of 13 spotted fever group serotypes tested. The location of this antigen on the rickettsial surface was demonstrated by immunoelectron microscopy with ferritin-labeled antibodies.
 ...
PMID:Biological properties of rabbit antibodies to a surface antigen of Rickettsia rickettsii. 640 67

Zipper particles are morphologically distinct transmembrane specializations of sperm tails. In freeze-fracture replicas of the guinea-pig sperm, they appear as an interdigitating double row of intramembranous particles running longitudinally within the plasma membrane of the principal piece. In thin section, zipper particles appear as an increase in electron density both above and below the bilayer. Zipper particles have been observed on a variety of both mammalian and non-mammalian species, suggesting that they have been conserved to serve an essential sperm function. As a first step towards biochemically characterizing guinea-pig zipper particles and towards developing a zipper isolation procedure, we performed an in situ lectin-binding study. Examination of nine gold- or ferritin-conjugated lectins revealed that three lectins, concanavalin A, Ricinus communis agglutinin I and wheatgerm agglutinin, bound to zipper particles. These lectin binding results suggest the presence of N-linked oligosaccharides within zipper particles. The results of the lectin binding study were then used in conjunction with a detergent solubilization procedure to identify potential zipper components. Detergent solubilization involved two non-ionic detergents: digitonin, which solubilized most of the plasma membrane, but left approximately two thirds of the zipper particles attached to the cytoskeleton, and Triton X-100, which solubilized the remaining zipper particles while leaving most other sperm structures intact. Within sodium dodecyl sulphate/polyacrylamide gels of the Triton-X-100-soluble fraction potential zipper particle components with the same lectin-binding characteristics as in situ zipper particles were identified.
 ...
PMID:Lectin binding to guinea-pig sperm zipper particles. 687 33

Anionic sites of rat epididymal spermatozoa were measured at pH 7.4 using tritiated polycationized ferritin. The spermatozoa from the caput region had 1.25 +/- 0.06 X 10(6) anionic sites per cell and a binding constant of 1.26 +/- 0.01 X 10(6) M-1. Spermatozoa from the cauda region had 1.50 +/- 0.09 X 10(6) anionic sites per cell and a binding constant of 4.84 +/- 0.82 X 10(6) M-1. The values were mean +/- s.d. The anionic sites were partly sensitive to treatments with neuraminidase, trypsin and Triton X-100.
 ...
PMID:Measurement of anionic sites of rat epididymal spermatozoa using tritiated polycationized ferritin. 688 40

Treatment of rat liver rough microsomes (3.5 mg of protein/ml) with sublytical concentrations (0.08%) of the neutral detergent Triton X-100 caused a lateral displacement of bound ribosomes and the formation of ribosomal aggregates on the microsomal surface. At slightly higher detergent concentrations (0.12-0.16%) membrane areas bearing ribosomal aggregates invaginated into the microsomal lumen and separated from the rest of the membrane. Two distinct classes of vesicles could be isolated by density gradient centrifugation from microsomes treated with 0.16% Triton X-100: one with ribosomes bound to the inner membrane surfaces ("inverted rough" vesicles) and another with no ribosomes attached to the membranes. Analysis of the fractions showed that approximately 30% of the phospholipids and 20-30% of the total membrane protein were released from the membranes by this treatment. Labeling with avidin-ferritin conjugates demonstrated that concanavalin A binding sites, which in native rough microsomes are found in the luminal face of the membranes, were present on the outer surface of the inverted rough vesicles. Freeze-fracture electron microscopy showed that both fracture faces had similar concentrations of intramembrane particles. SDS PAGE analysis of the two vesicle subfractions demonstrated that, of all the integral microsomal membrane proteins, only ribophorins I and II were found exclusively in the inverted rough vesicles bearing ribosomes. These observations are consistent with the proposal that ribophorins are associated with the ribosomal binding sites characteristic of rough microsomal membranes.
 ...
PMID:Recovery of ribophorins and ribosomes in "inverted rough" vesicles derived from rat liver rough microsomes. 706 49

Microinjection of polyclonal sheep anti-vimentin IgGs purified by affinity chromatography into a rat fibroblastoid line leads to a specific reorganization of the cytoskeleton. Immunofluorescence microscopy shows that cytoplasmic microtubules and microfilaments are unaffected by intermediate filaments collapse and are collected into a tight perinuclear cap containing antibody-crosslinked vimentin filaments. The crosslinking was further documented by electron microscopy after treatment with Triton X-100 and ferritin-labelled anti-sheep IgGs. Inspite of the presence of the caps, which are retained for about 30 h, cells show a normal morphology and are locomotive. The collapsed intermediate filaments do not interfere with subsequent mitosis or with cytokinesis. After mitosis the capped filaments can be distributed either to both daughter cells or to only one of the two daughter cells.
 ...
PMID:Coiling of intermediate filaments induced by microinjection of a vimentin-specific antibody does not interfere with locomotion and mitosis. 719 76


<< Previous 1 2 3 Next >>