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  • 1
    Electronic Resource
    Electronic Resource
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 78 (1995), S. 6189-6192 
    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
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Inorganic chemistry 24 (1985), S. 2604-2608 
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 16404-16411 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Conglutinin is a mammalian C-lype lectin which agglutinates iC3b-coated erylhrocytes, Ingram [13] found that euglobulin from bovine serum may confer partial protection against experimental infections in mice. We now present evidence that the protective activity in euglobulin against infections of BALB/c mice with Salmonella typhimurium is mediated by conglutinin. Conglutinin also demonstrated antibacterial activity against E. coli and S. typhimurium in vitro. The expression of this activity required the presence of heat-labile serum factors and peritoneal exudate or spleen cells, but not antibodies to the bacteria. Antibacterial activity was also demonstrated when the bacteria were prelreated with serum at 37°C before incubation with conglutinin and cells. The activity of conglutinin was not observed when factor I-deficient or EDTA-treated serum was used instead of normal serum. The active peritoneal exudate or spleen cells showed adherence to plastic.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 33 (1991), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The highly glycosylated envelope glycoprotein (gpl60) of human immunodeficiency virus (HIV) interacts with the CD4 molecule present on the membrane of CD4+ cells and is involved in the pathobiology of HIV infection. Lectins bind glycoproteins through non-covalent interactions with specific hexose residues. The mammalian C-type lectin bovine conglutinin was examined for its ability to interact with recombinant gpl60 (rgpl60) produced in vaccinia virus-infected BHK21 cells. Specific binding of conglutinin to rgp160 was demonstrated by ELISA. The interaction of bovine conglutinin with rgp160 was calcium-dependent, which is characteristic of the binding of a C-type lectin to its ligand, and the binding was inhibited in a dose-dependent manner with A-acetyl-D-glucosamine. Deglycosylation of rgpl60 abrogated the conglutinin binding. In addition, conglutinin exerted a dose-dependent inhibition of the binding of rgp160 to the CD4 receptor on CEM 13 cells, as demonstrated by FACS analyses. These results indicate that conglutinin may inhibit the infection with HIV-1 through its interaction with the viral envelope glycoprotein.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 20 (1984), S. 0 
    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
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 22 (1985), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Human lymphokine-activated monocytes release a cytotoxic protein factor (CF). The cytostatic activity of CF was potentiated by the DNA and RNA synthesis inhibitors actinomycin D, daunomycin, and mitomycin C. These inhibitors increased the sensitivity for detecting CF approximately 10-fold, and this is of great practical value when assaying CF. The CF-potentialing inhibitors had a similar effect on the cell cycle distribution in that they all induced an accumulation of cells in the S and G2 phases of the cell cycle. Cytolytic activity was shown to be associated with CF, and this activity was also greatly potentiated by daunomycin and actinomycin D. The two other inhibitors studied, cycloheximide and 5-fIuorouracil (5-FU), had an adverse effect on the cytostatic activity of CF. These two inhibitors reduced the sensitivity of the assay for CF about fivefold. Cycloheximide had no apparent effect on the relative cell cycle distribution, whereas 5-FU induced an accumulation of cells in the G1 phase. Of the inhibitors studied, only those that induced an accumulation of cells in the S and G2 phases of the cell cycle potentiated the cytotoxic activity of CF. suggesting that CF may preferentially act in these parts of the cell cycle.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 133 (1966), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 41 (1995), S. 0 
    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
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 43 (1996), S. 0 
    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
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