Immune reactions in polysaccharide media. Investigation on complex-formation between some polysaccharides, albumin and immunoglobulin G.
Serum albumin and immunoglobulin G were chromatographed on columns of dextran, hyaluronate and chondroitin 4-sulphate. The partition of the two proteins between hyaluronate and buffer was also measured by equilibrium dialysis. The results accord with the view that there is no complex-formation between the polysaccharides and the proteins in 0.05m-phosphate buffer, pH7.4, containing sodium chloride (0.1m). The observations support the hypothesis that the previously described polysaccharide enhancement of the precipitin reaction is due to exclusion and not to non-specific complex-formation.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002807:Chondroitin; D002845:Chromatography; D002850:Chromatography, Gel; D003911:Dextrans; D003956:Dialysis; D006801:Humans; D006820:Hyaluronic Acid; D006863:Hydrogen-Ion Concentration; D007120:Immunochemistry; D007074:Immunoglobulin G; D011134:Polysaccharides; D011234:Precipitins; D011817:Rabbits; D012709:Serum Albumin; D012711:Serum Albumin, Radio-Iodinated; D013431:Sulfates
D003911:Dextrans; D007074:Immunoglobulin G; D011134:Polysaccharides; D011234:Precipitins; D012709:Serum Albumin; D012711:Serum Albumin, Radio-Iodinated; D013431:Sulfates; D006820:Hyaluronic Acid; D002807:Chondroitin