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  • 1
    Electronic Resource
    Electronic Resource
    Effects of anti-insulin antibody on insulin binding to liver membranes: evidence against antibody-induced enhancement of insulin binding to the insulin receptor (1986)
    Springer
    Diabetologia 29 (1986), S. 447-452 
    Details
    ISSN: 1432-0428
    Keywords: Anti-insulin antibody ; insulin receptor ; insulin binding ; cross-linking ; disuccinimidyl suberate ; Fcy receptor ; liver membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In the presence of anti-insulin antibody, 2- to 3-fold enhancement of 125I-insulin binding to liver membranes was observed when binding was estimated by the radioactivity of 125I-insulin bound to the membrane pellets. However, after 125'I-insulin was covalently cross-linked to liver membranes using disuccinimidyl suberate in the presence of anti-insulin antibody, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography showed that 125I-insulin bound to the α-subunit of the insulin receptor was inhibited by antiinsulin antibody in an dose-dependent manner. More importantly, at an anti-insulin antibody dilution range between 1:50 and 1:5,000, sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed two 125I-labelled bands of mol wt 62,000 and 27,000, while only one band of mol wt 130,000 was revealed in the absence of anti-insulin antibody. These Mr=62,000 and Mr=27,000 bands were found to be the heavy and the light chain of anti-insulin IgG molecules respectively. Pepsin digested anti-insulin serum had only an inhibitory effect on 125I-insulin binding to liver membranes. Non-immunized guinea pig serum or IgG completely abolished the enhanced effect of anti-insulin antibody. Further, this enhanced effect was inhibited by Fc fragment-specific anti-IgG serum or H&L-chain-specific anti-IgG serum in a dosedependent manner. Protein A also inhibited the effect of antiinsulin antibody. In IM-9 lymphocytes and human red blood cell ghosts, which have no Fcy receptors, enhancement of insulin binding was not observed in the presence of anti-insulin antibody. These data suggest that anti-insulin antibody-induced enhancement of insulin binding to liver membranes is not due to the enhanced binding to the insulin receptor itself but probably due to the binding of insulin-anti-insulin antibody complex to the Fcγ receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00506537
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Adhesive effect of high density polyethylene gels on polyethylene moldings (1989)
    Springer
    Colloid & polymer science 267 (1989), S. 500-505 
    Details
    ISSN: 1435-1536
    Keywords: Adhesion ; gel ; decalin ; tetralin ; highdensitypolyethylene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Adhesive effect of polyethylene moldings by use of high density polyethylene gels in organic solvents such as decalin, tetralin, ando-dichlorobenzene was investigated by shearing tests, electron microscope, and DSC measurements. All of the gels showed such a strong adhesive strength over 36 kg/cm2 that polyethylene plates of 3 mm in thickness gave rise to necking sufficient for practical use, when heated at 120 °C for 2 h. In particular, the gel in tetralin showed a strong adhesive strength when heated at 110 °C. It was found that adhesive strength increases with the heating temperature; the temperatures at which adhesive strength begins to increase differ depending on the type of polyethylene sample and solvent. It is apparent that polyethylene gels exhibit an adhesive effect when they are heated at higher temperatures than the gel melting temperatures, and that the closer the SP values of solvents used for the gelation are to the molded polyethylene, the stronger the adhesion of the polyethylene molding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01416055
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    Paper (German National Licenses)
    Fulltext
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