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

Cell surface hydrophobicity of Mycoplasma hyopneumoniae was evaluated by phase partitioning in a hydrocarbon-aqueous mixture, by hydrophobic interaction chromatography, and by salting out with ammonium sulfate. Results obtained by use of these techniques gave evidence that the cell surface of M hyopneumoniae is weakly hydrophobic, compared with strongly hydrophobic Staphylococcus aureus Cowan I and hydrophilic Klebsiella pneumoniae. After treatment of the organisms with trypsin, M hyopneumoniae became less hydrophobic as measured by hydrophobic interaction chromatography. Significant changes in hydrophobicity were not seen after periodate treatment. Electron microscopy of M hyopneumoniae treated with polycationic ferritin revealed an intermediate, compact, unlabeled layer between the cytoplasmic membrane and an external, heavily labeled layer. Electron microscopy of ferritin-labeled M hyopneumoniae after treatment with trypsin or periodate revealed the intermediate layer to be composed of a trypsin-sensitive protein(s). The outer layer was made of periodate-sensitive carbohydrate(s). Therefore, it appears that proteins in the intermediate layer confer at least part of the total hydrophobicity of the mycoplasmal cell and may contribute to adherence of M hyopneumoniae to target respiratory cells by hydrophobic interactions.
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PMID:Morphologic features and hydrophobicity of the cell surface of Mycoplasma hyopneumoniae. 132 25

The indirect immunoferritin labeling method was used to localize the membrane-bound respiratory nitrate reductase in membrane vesicles and protoplasts or sphereplasts of Bacillus licheniformis and Klebsiella aerogenes, respectively. For a comparison of the labeling of the various vesicle preparations, which differed not only in size but also in the percentage of inside-out orientation, a quantification of the results was needed to circumvent the problem of non-specifically bound ferritin. From the results of sidedness of the nitrate reductase in the cytoplasmic membrane of the above-mentioned bacteria was determined as being cytoplasmic in B. licheniformis and as transmembranous in K. aerogenes.
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PMID:Immunoferrin labeling of respiratory nitrate reductase in membrane vesicles of Bacillus licheniformis and Klebsiella aerogenes. 700 23

Radioimmunoassay with calf and cow vitreous humour-I125 and rabbit antivitreous humour serum has been employed to investigate the immunological cross-reactivity of vitreous humour with bacterial and mammalian tissue antigens. Klebsiella ultrasonicate preparation at a dose fo 10 000 micrograms/ml was found to inhibit the binding of vitreous humour by 25-100% (p less than 0.001), compared with an inhibition of 5-30% by a similar quantity of E. coli ultrasonicate preparation. Equivalent amounts of Streptococcus pyogenes antigen, bovine haemoglobin, and hyaluronic acid had no inhibitory effect, while horse spleen ferritin was found to inhibit vitreous humour binding between 0 and 10%. These results indicate that klebsiella micro-organisms have antigens which partially resemble some eyeball components. It is suggested that acute anterior uveitis of ankylosing spondylitis may be produced by anti-Gram-negative bacterial antibodies binding to cross-reacting eye antigens.
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PMID:Uveitis, vitreous humour, and klebsiella. II. Cross-reactivity studies with radioimmunoassay. 701 60

In plasma clots the presence of ferritin-antiferritin complexes interferes with the bactericidal powers of polymorphs against Klebsiella pneumoniae and Escherichia coli. Equivalent concentrations of apoferritin-antiferritin complexes, which lack Fe, do not have this effect and it is therefore suggested that the iron-binding capacity of lactoferrin in polymorphs plays an essential role in the bactericidal power of the cell. Similar results were obtained in vivo where ferritin-antiferritin complexes cause a high mortality in otherwise non-lethal infections. Evidence suggests that it is the iron in the ferritin which is responsible for the rapid intracellular bacterial growth and that lactoferrin normally plays an important protective role within the polymorphs.
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PMID:Abolition of the bactericidal function of polymorphs by ferritin-antiferritin complexes. 704 83

A strain of Klebsiella oxytoca, isolated from acid pyrite-mine drainage, characteristically produces a ferric hydrogel, consisting of branched heptasaccharide repeating units exopolysaccharide (EPS), with metal content of 36 wt%. The high content of iron in the EPS matrix cannot be explained by a simple ferric ion bond to the sugar skeleton. The bio-generated Fe-EPS is investigated by X-ray absorption spectroscopy. Fe K-edge XANES analysis shows that iron is mostly in trivalent form, with a non-negligible amount of Fe(2+) in the structure. The Fe EXAFS results indicate that iron in the sample is in a mineralized form, prevalently in the form of nano-sized particles of iron oxides/hydroxides, most probably a mixture of different nano-crystalline forms. TEM shows that these nanoparticles are located in the interior of the EPS matrix, as in ferritin. The strain produces Fe-EPS to modulate Fe-ions uptake from the cytoplasm to avoid iron toxicity under anaerobic conditions. This microbial material is potentially applicable as iron regulator.
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PMID:XAS analysis of a nanostructured iron polysaccharide produced anaerobically by a strain of Klebsiella oxytoca. 2258 84