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  • 1
    Electronic Resource
    Electronic Resource
    Photoinduced synthesis of porous silicon without anodization (1995)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 78 (1995), S. 6189-6192 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: An easy and very reproducible method to produce porous silicon by light-stimulated etching of crystalline silicon in HF is described, and the formation mechanism is discussed in terms of carrier diffusion and band bending near the surface. The method avoids the use of electrodes and electrochemical etching. The photosynthesized porous silicon shows bright photoluminescence. Spectra recorded at room temperature for n-type as well as p-type silicon are presented. © 1995 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.360564
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  • 2
    Electronic Resource
    Electronic Resource
    Gramicidin Channel Function Does Not Depend on Phospholipid Chirality (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 16404-16411 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00050a022
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  • 3
    Electronic Resource
    Electronic Resource
    Purification of Cytostatic Protein Factors Released from Human Monocytes (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 20 (1984), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Human monocyles release cytostatic protein factors (CF) upon activation with lymphokines und lipopolysacchairide. CF has been purified from monocyte supernatants by ion-exchange chromatography. chromatofocusing and gel filtration, and this resulted in a 10,000-fold reduction in the amount of protein in the purified CF preparation compared to the amount in the monocyte supernatant. About 5% of the eytostatic activity was recovered after purification. CF constitutes a population of proteins heterogeneous with respect to ionic charge and differing in their isoelectric points, since CF eluted as a broad peak both upon ion-exchange chromatography and chromatofocusing. The isoelectric points of the CF proteins were determined by chromatofocusing to be between 6.0 and 5.0. The molecular weight of CF as determined by gel filtration was in the range of 45,000 to 35,000 daltons. Only one monocyte-secreted protein with a molecular weight of 40,000 was detected upon sodium dodecyl sulphate-polyacrylamide gel electrophoresis of proteins in the purified CF preparations obtained after the final gel filtration step, und this protein may consequently be CF. If the 40,000-dalton protein is CF. one may estimate that about 106 monocytes produced roughly 0.1 μg CF upon activation and that significant cytostasis may be detected with less than nanogram quantities of CF.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1984.tb01008.x
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  • 4
    Electronic Resource
    Electronic Resource
    Native Human Serum Amyloid P Component is a Single Pentamer (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 41 (1995), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Serum amyloid P component (SAP) and C-reactive protein (CRP) are members of the pentraxin protein family. SAP is the precursor protein to amyloid P component present in all forms of amyloidosis. The prevailing notion is that SAP in circulation has the form of a double pentameric molecule (decamer) whereas CRP is a single pentameric molecule.We have investigated by gel permeation chromatography the Mr of SAP in freshly collected human serum and of SAP purified by carbohydrate affinity chromatography and anion exchange chromatography. SAP was monitored by quantitative immunoelectrophoresis and ELISA. and SAP peak fractions were analysed by use of SDS-PAGE, Western blotting, and electron microscopy. The results indicate that native SAP circulates as a single pentamer, a part of which forms complexes with C4b-binding protein. The properties of SAP changed during purification as indicated by rocket immuno-electrophoresis and electron microscopy. Thus, electron micrographs of purified SAP showed a predominance of decamers. However, the decamer form of SAP reversed to single pentamers when purified SAP was incorporated into SAP-depleted serum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1995.tb03562.x
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation and Characterization of Porcine Mannan-Binding Proteins of Different Size and Ultrastructure (1996)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 43 (1996), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The authors report on the purification and characterization of mannan-binding proteins (MBP) isolated from porcine serum. The MBPs were purified by use of PEG precipitation, affinity chromatography on mannan-Sepharose, protein A- and anti-porcine IgM-Sepharose followed by gel filtration. The MBP proteins were collagenase sensitive and showed γ1-γ2-electrophoretic mobility. The MBP designated pMBP-28 had a molecular mass of 28 kDa when analysed on SDS-PAGE under reducing conditions and eluted corresponding to a molecular mass of approximately 700 kDa on gel filtration chromatography. Electron micrographs of pMBP-28 revealed an oligomeric protein similar to rodent MBP-A and human MBP but with a predominance of penta- and hexameric molecules. Another protein designated pMBP-27 was composed of peptides of 27 kDa and had an Mr of 300–350 kDa on gel filtration chromatography. Electron microscopy of pMBP-27 showed dimer and trimer molecules; the trimers without distinct stalk regions. The N-terminal 26 (pMBP-27) and 24 (MBP-28) amino acid residues showed 54% and 58% identity with human MBP. pMBP-28 showed a higher degree of sequence similarity to rat and mouse MBP-A (60% identity) than to mouse and rat MBP-C (41–45% identity). Both pMBPs exhibited Ca2+-dependent binding to D-mannose immobilized on agarose but no significant binding to N-acetyl-D-glucosamine- or fucose-agarose. The results further suggested the presence of a third pMBP which copurified with pMBP-27 but this protein was not sequenced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-39.x
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  • 6
    Electronic Resource
    Electronic Resource
    Gramicidin Channels (1984)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physiology 46 (1984), S. 531-548 
    Details
    ISSN: 0066-4278
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ph.46.030184.002531
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  • 7
    Electronic Resource
    Electronic Resource
    Serum Amyloid P Component Binds to Influenza A Virus Haemagglutinin and Inhibits the Virus Infection In Vitro (1997)
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 46 (1997), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Serum amyloid P component (SAP) is a member of the phylogenetically conserved and structurally related group of proteins called pentraxins. SAP exhibits multispecific calcium-dependent binding to oligosaccharides with terminal N-acetyl-galactosamine, mannose and glucuronic acid. The authors report that SAP can bind to influenza A virus and inhibit agglutination of erythrocytes mediated by the virus subtypes H1N1, H2N2 and H3N2. SAP also inhibits the production of haemagglutinin (HA) and the cytopathogenic effect of influenza A virus in MDCK cells. The binding of SAP to the virus requires physiological calcium concentrations and is blocked by specific SAP antibodies. Denaturated and renaturated SAP retained inhibition of HA. Electron microscopy shows Ca2+-dependent binding of SAP to spikes on the viral envelope and immunoblotting indicates that SAP binds to a 50–55 kDa peptide corresponding to the mass of the HA1 peptide. Of several monosaccharides tested only D-mannose interfered with SAP's inhibition of both HA and infectivity. The glycosaminoglycans heparan sulfate and heparin, which bind SAP, reduced SAPs binding to the virus. The results indicate that the inhibition by SAP is due to steric effects when SAP binds to terminal mannose on oligosaccharides localized close to the sialic acid-binding site of the HA trimer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1997.d01-147.x
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  • 8
    Electronic Resource
    Electronic Resource
    Binding of Complement Proteins C1q and C4bp to Serum Amyloid P Component (SAP) in Solid Contra Liquid Phase (1996)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 44 (1996), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Serum amyloid P component (SAP), a member of the conserved pentraxin family of plasma proteins, binds calcium dependently to its ligands. The authors investigated SAPs interaction with the complement proteins C4b binding protein (C4bp) and C1q by ELISA, immunoelectrophoresis and electron microscopy. Binding of these proteins to SAP was demonstrated when SAP was immobilized using F(ab′)2 anti-SAP, but not when SAP reacted with these proteins in liquid phase; thus the binding to human SAP was markedly phase state dependent. Presaturation of solid phase SAP with heparin, which binds SAP with high affinity, did not interfere with the subsequent binding of C4bp or C1q to SAP. In contrast, collagen I and IV showed partial competition with the binding of C1q to SAP. Using fresh serum, immobilized native SAP bound C4bp whereas binding of C1q/C1 could not be demonstrated. Altogether the results indicate that firm binding of C1q and C4bp to SAP requires that SAP is presented on a solid phase, that C1q and C4bp react with sites distinct from the heparin binding site, and that C1q and collagen I share binding sites on SAP. Immobilized native SAP, aggregated SAP and SAP-heparan-sulphate complexes induced no detectable complement activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-326.x
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  • 9
    Electronic Resource
    Electronic Resource
    Mannan-Binding Protein Forms Complexes with α-2-Macroglobulin. A Proposed Model for the Interaction (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 42 (1995), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We report that α-2-macroglobulin (α2M) can form complexes with a high molecular weight porcine mannan-binding protein (pMBP-28). The α2M/pMBP-28 complexes were isolated by PEG-precipitation and affinity chromatography on mannan-Sepharose, protein A-Sepharose and anti-IgM Sepharose. The occurrence of α2M/pMBP-28 complexes was further indicated by crossed immunoelectrophoresis and by use of an anti-α2M affinity column and chelating Sepharose loaded with Zn2+. The eluates from these affinity columns showed α2M subunits (94 and 180 kDa) and pMBP subunits (28 kDa) in SDS-PAGE, which reacted with antibodies against α2M and pMBP-28, respectively, in Western blotting. Furthermore, the α2M/pMBP-28 complexes were demonstrated by electron microscopy, Fractionation of pMBP-containing D-mannose eluate from mannan-Sepharose on Superose 6 showed two protein peaks which reacted with anti-C1 s antibodies in ELISA, one of about 650–800 kDa, which in addition contained pMBP-28 and anti-α2M reactive material, the other with an Mr of 100–150 kDa. The latter peak revealed rhomboid molecules (7 × 15 nm) in the electron microscope and a 67 kDa band in SDS-PAGE under reducing conditions. This band was also seen in eluates from the anti-α2M and chelating Sepharose columns. Based on these observations and previous findings by other investigators of a serine protease with about 67 kDa subunits which copurifies with human MBP we propose a model for the interaction of pMBP-28 with α2M.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1995.tb03670.x
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  • 10
    Electronic Resource
    Electronic Resource
    Batrachotoxin-Modified Sodium Channels in Lipid Bilayers (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 435 (1984), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1984.tb13879.x
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