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  • 1
    Electronic Resource
    Electronic Resource
    Purification and reconstitution into liposomes of an integral membrane protein conferring immunity to colicin A (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 60 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The immunity protein to colicin A protects producing cells from the action of this pore-forming toxin. It is located into the cytoplasmic membrane. This protein has been ‘tagged’ with an epitope from the colicin A protein for which a monoclonal antibody is available. The fusion protein (named VL1) has been purified after extraction from the membrane in two steps using a chromatofocusing and an immunoadsorbant chromatography. The purified protein has then been reconstituted into lipid vesicles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03453.x
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  • 2
    Electronic Resource
    Electronic Resource
    Localization of hydrogenase in Desulfovibrio gigas cells (1991)
    Springer
    Archives of microbiology 155 (1991), S. 579-586 
    Details
    ISSN: 1432-072X
    Keywords: Desulfovibrio ; Hydrogenase activity ; Hydrogenase localization ; Immunogold labelling ; Bioenergetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The localization of hydrogenase protein in Desulfovibrio gigas cells grown either in lactate-sulfate or hydrogen-sulfate media, has been investigated by subcellular fractionation with immunoblotting and by electron microscopic immunocytochemistry. Subcellular fractionation experiments suggest that no integral membrane-bound hydrogenase is present in D. gigas. About 40% of the hydrogenase activity could be extracted by treatment of D. gigas cells with Tris-EDTA buffer. The rest of the soluble hydrogenase activity (50%) was found in the soluble fraction which was obtained after disruption of Tris-EDTA extracted cells and high speed centrifugation. Both soluble hydrogenase fractions purified to homogeneity showed identical molecular properties including the N-terminal aminoacid sequences of their large and small subunits. Polyacrylamide gel electrophoresis of the proteins of the subcellular fractions revealed a single band of hydrogenase activity exhibiting the same mobility as purified D. gigas hydrogenase. Western blotting carried out on these subcellular fractions revealed crossreactivity with the antibodies raised against (NiFe) hydrogenase. The lack of crossreactivity with antibodies against (FE) or (NiFeSe) hydrogenases, indicated that only (NiFe) type hydrogenase is present in D. gigas. Immunocytolocalization in ultrathin frozen sections of D. gigas cells grown either in lactate-sulfate, pyruvate-sulfate or hydrogen-sulfate media showed only a (NiFe) hydrogenase located in the periplasmic space. The bioenergetics of D. gigas are discussed in the light of these findings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245353
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Aminopeptidase N is a marker for the apical pole of porcine thyroid epithelial cells in vivo and in culture (1981)
    Springer
    Cell & tissue research 221 (1981), S. 137-146 
    Details
    ISSN: 1432-0878
    Keywords: Aminopeptidase ; Thyroid ; Thyroid cell ; Membrane marker ; Polarization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary An aminopeptidase N has been detected by immunofluorescence in the apical plasma membrane of porcine thyroid cells, facing the follicular lumen. Freshly isolated cells obtained by tissue trypsinization, lose their polarity and exhibit a homogeneous enzyme distribution over the whole plasma membrane. In thyrotropin-stimulated cultured cells organized into follicles, the enzyme is localized in the apical cell pole. In monolayer cells, on the other hand, the enzyme is distributed over the whole surface facing the medium. In both types of cultures fluorescence is also observed in intracytoplasmic organelles. In vivo, aminopeptidase is a marker of the apical part of the thyroid plasma membrane, but its in vitro localization depends upon cell differentiation related to the culture conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00216576
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    Paper (German National Licenses)
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