A hapten-induced conformational change accompanies the cryoprecipitation of an immunoglobulin.
By simultaneous spectroscopic measurements (absorbance, light scattering, fluorescence and circular dichroism) the temp-dependent behavior of a cryoglobulin, the mouse monoclonal immunoglobulin G to N-acetyllactosamine, has been observed. The results show that a hapten-induced conformational change in the structure of a cryoglobulin can accompany its intermolecular association. This association of the immunoglobulin increases after hapten saturation of its two antigen-combining sites.
D000606:Amino Sugars / Q000276:immunology; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002942:Circular Dichroism; D003450:Cryoglobulins / Q000276:immunology*; D006241:Haptens / Q000276:immunology*; D007074:Immunoglobulin G / Q000276:immunology*; D008027:Light; D051379:Mice; D011487:Protein Conformation; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D013057:Spectrum Analysis; D013696:Temperature
D000606:Amino Sugars; D000911:Antibodies, Monoclonal; D003450:Cryoglobulins; D006241:Haptens; D007074:Immunoglobulin G; C000458:N-acetyllactosamine