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)

The immunochemical method has been proposed to indicate the adenin compounds in isolated myofibrils of striated muscle. Adenosine--containing antigen was prepared by coupling adenosine with bovine serum albumin (adenosine--BSA). Antibodies against adenosine--BSA were labelled by ferritin. The sites of the antigen antibody reaction were marked by localization of ferritin molecules. Ferritin antibodies were found to concentrate in the following sarcomere sites: M and Z bands, N-lines and terminal cisternae of sarcoplasmic reticulum near the Z-bands.
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PMID:[Localization of adenine components in chick myofibrils by the ferritin antibody technic]. 43 20

Electron microscopy cytochemistry has been used to study the cytoplasmic location of liposomes and lipid vesicles following specific antibody-dependent phagocytosis. The vesicle compositions were 94-99 mol% 'fluid' lipid (egg phosphatidylcholine or dimyristoylphosphatidylcholine at 37 degrees C or 'solid' lipid (dipalmitoylphosphatidylcholine at 37 degrees C). In some cases, 4 mol% phosphatidylserine was included in the vesicle membrane so as to vary the surface charge density. These vesicles undergo specific antibody-dependent phagocytosis by RAW264 macrophages when the lipid membranes contain 1-2 mol% dinitrophenyl lipid hapten in the presence of rabbit anti-dinitrophenyl IgG antibody. Internalized lipid vesicles can be visualized with the electron microscope when ferritin is trapped in the internal aqueous compartments prior to internalization. The lipid vesicles were demonstrated to be internal to the macrophage plasma membranes by selectively staining the plasma membranes with Ruthenium red. The cytoplasmic location of vesicles and liposomes was studied by electron microscopic staining for activities of the following enzymes: (1) acid phosphatase; (2) inorganic trimetaphosphatase; (3) adenosine triphosphatase; and (4) glucose-6-phosphatase. The first two enzymatic activities were found in association with ferritin-containing vesicles after antibody-dependent phagocytosis, showing the formation of vesicle-containing phagolysosomes. Adenosine triphosphatase and glucose-6-phosphatase were primary not associated with the vesicles, suggesting a minimal association of vesicles with plasma membrane, Golgi, endoplasmic reticulum and perinuclear cisternae. Phagosome-lysosome fusion did not appear to depend on the type of target lipid vesicle or liposome, on the 'fluidity' of the target membrane, or the presence of phosphatidylserine in the target membrane.
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PMID:Cytochemical study of liposome and lipid vesicle phagocytosis. 668 37

Chromium(VI) reduction was studied in a system composed of reduced nicotinamide adenine dinucleotide phosphate-cytochrome P450 oxidoreductase (NADPH-P450 reductase) and different iron chelators and iron sources. In an aerobic phosphate buffer containing iron(II), chromium(VI) was not reduced by the Fe2+ probably because of spontaneous autoxidation of Fe2+, but freshly made Fe2+, added directly to a CrVI-containing buffer, reduced CrVI. Under anaerobic conditions, iron(II) reduced chromium(VI) stoichiometrically. A systemic containing ethylenediaminetetraacetic acid (EDTA)-Fe3+, NADPH-P450 reductase and NADPH effectively reduced chromium(VI) anaerobically. Under aerobic conditions this reaction was inhibited by about 45%. Adenosine diphosphate (ADP)-Fe3+, which is a poor acceptor of electrons from NADPH-P450 reductase, reduced chromium(VI) only marginally, Mannitol slightly increased the aerobic CrVI reduction. Addition of superoxide dismutase and catalase, which both regenerate some O2, led to inhibition of CrVI reduction. Ferritin, NADPH-P450 reductase and the iron chelators, EDTA and citrate, reduced CrVI, indicating mobilization of Fe2+ from ferritin. Low levels of EDTA (55 mumol l-1) and citrate (100 mumol l-1) in contrast to high levels (5 mmol l-1) did not increase CrVI reduction in microsomes. Using 4-(2-hydroxyethyl)-1-piperazineethane sulfonic acid buffer instead of phosphate buffer, the CrVI-reducing activity was increased.
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PMID:The role of iron chelators and oxygen in the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P450 oxidoreductase-dependent chromium(VI) reduction. 774 Dec 58