THE INFLUENCE OF IMMUNOGLOBULIN (IGG) ON THE ASSEMBLY OF FIBRIN GELS

  • 1 January 1983
    • journal article
    • research article
    • Vol. 101  (4) , 545-552
Abstract
The presence of Ig alters the network structure of gels formed from purified fibrinogen. Turbidity measurements were used to calculate the effect of increasing concentrations of Ig on the mass-length ratio of fibrin fibers composing the gels. Normal pooled, human IgG reduced the mass-length ratio of fibrin fibers composing the gel from 7 .times. 1012 daltons/cm with no Ig to 1 .times. 1012 in the presence of 40 mg/ml. Monoclonal IgG.kappa. was more effective in the reduction of the mass-length ratio than normal IgG. The Ig apparently decreases lateral association of fibrin protofibrils. As the mass-length ratio decreased, the rigidity of the gels increased as the Ig concentration was elevated (1.2 dynes/cm2 with no Ig to 2.9 at 15 mg/ml). Since the fibrin fiber diameters were decreased, the number of interfiber crosslinks must have been increased to explain the increase in rigidity. Antifibrinogen, antifibrin intermediate and antithrombin antibody activity of the Ig is unlikely.