Abstract
Abstract Factors influencing the precipitation of a mixed cryoglobulin formed by the interaction of a Waldenström macroglobulin antibody (IgMSie) with its antigen (human IgG) have been studied. Binding of FabµSie fragments to a G1, κ myeloma protein in the analytical ultracentrifuge showed that the IgG antigen was effectively univalent. Consequently, IgM(IgG)10 is the largest potential complex that can form in this system. Experiments performed by the method of equilibrium molecular sieving demonstrated that primary affinity of antibody combining site for antigenic determinant exhibits modest temperature dependence similar to that observed in other antigen-antibody systems. Solvent ionic strength and change in pH near neutrality did not significantly alter the association constant. By contrast, precipitation of the IgMSie-IgG complex was profoundly affected by variation in temperature, ionic strength, and pH. Larger complexes were required for precipitation to occur when the reaction was carried out under non-optimal environmental conditions or when certain IgG antigens were employed. These results indicate that the cryoprecipitating phenomenon is explicable by the finite size and limited solubility of the IgM-IgG immune complexes.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
