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  • 1
    Electronic Resource
    Electronic Resource
    In situ immunoradiometric assay of fibrinogen adsorbed to artificial surfaces (1984)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 18 (1984), S. 547-559 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: An in situ immunoradiometric assay was devised to quantitate human fibrinogen deposited on hemodialysis membrane, Cuprophane, from in vitro exposure to fibrinogen solution and from ex vivo extracorporally clinical use. The method requires a monospecific 125I-labeled antifibrinogen-IgG purified by DEAE chromatography and immunoadsorption. The labeled antifibrinogen IgG was shown to react specifically with fibrinogen adsorbed and immobilized (by glutaraldehyde) on Cuprophane. Other plasma proteins such as human albumin, IgG, or α-thrombin, adsorbed singly or coadsorbed with fibrinogen on the surface did not seem to affect the fibrinogen-antifibrinogen reaction. The presence of blood cells such as platelets and granulocytes with fibrinogen on Cuprophane reduced only slightly the uptake of 125I-antifibrinogen-IgG. The examination of fibrinogen-fibrin deposition on clinically used Cuprophane by this technique and by autoradiography of the same material following 125I-antifibrinogen-IgG conjugation indicated that the deposition of fibrinogen was heavy and heterogeneous. We concluded that this in situ method may be useful to monitor fibrinogen-fibrin deposition and adsorption of other plasma proteins that occur under in vitro, ex vivo, and in vivo conditions.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820180508
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Adsorption and reactivity of human prothrombin to artificial surfaces (1984)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 18 (1984), S. 695-705 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Human prothrombin in Tyrode's solution, in mock plasma (albumin, fibrinogen, and IgG mixture), and in citrated plasma adsorbs to Cuprophane, polyvinylchloride, and polyacrylonitrile surfaces. The adsorption of prothrombin is maximal in Tyrode's solution and minimal in plasma. The surface concentrations of prothrombin are highest on polyacrylonitrile, second on polyvinylchloride, and lowest on Cuprophane at all prothrombin concentrations tested in the bulk solution. Qualitative tests show that prothrombin adsorbed to polyvinylchloride can be activated by Taipan snake venom to generate thrombin that clots fibrinogen. However, more quantitative tests indicate that only part of the adsorbed prothrombin on all three materials can be activated to form thrombin exhibiting amidolytic activity. The partial reactivity of adsorbed prothrombin is further confirmed by release of 125I-peptide from surface bound 125I-prothrombin after treatment with Australian Taipan snake venom. Prothrombin bound to Cuprophane seems to promote granulocyte adhesion, but has no effect on platelet adhesion.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820180610
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Immunochemical detection by specific antibody to thrombin of prothrombin conformational changes upon adsorption to artificial surfaces (1985)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 19 (1985), S. 813-825 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Polyclonal antihuman α-thrombin antibodies produced in rabbits reacted minimally (〈0.05%) in solution with human prothrombin. However, when prothrombin was adsorbed to artificial surfaces such as polyvinyl chloride (PVC), the crossreactivity of surface-bound prothrombin with antibody IgG to thrombin (〉95% purity) was shown to be significantly enhanced. On PVC, the molar ratios of antibody IgG to thrombin/prothrombin approached the same level as that of antibody IgG to thrombin/thrombin when thrombin was adsorbed to the same material. The analyses of antigen-antibodies interaction, in solution with a direct binding assay by immune precipitation at high-speed centrifugation (160,000 g, 30 min), and on solid-phase PVC, were accomplished by use of double-labeling technique, i.e., 131I-thrombin (or 131I-prothrombin) and 125I-antibody IgG to thrombin. The results appear to suggest that prothrombin adsorption to PVC has resulted in some molecular conformational changes so that immunologically the adsorbed prothrombin resembles that of adsorbed thrombin on the same PVC surface.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820190707
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    Paper (German National Licenses)
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