Purification of cold agglutinins from patients with chronic cold haemagglutinin disease. Evidence of their homogeneity from starch gel electrophoresis of isolated light chains.

A method is described for the large scale purification of serologically active high-titre cold agglutinins from the sera of patients with chronic cold haemagglutinin disease. Eighteen purified cold agglutinins have been reduced and alkylated and separated into heavy and light chain pools by Sephadex G-100 filtration. The isolated light chains were examined by alkaline urea starch gel electrophoresis and found to be far more homogeneous than normal light chains and comparable in some cases to Bence Jones light chains. However, light chains from different cold agglutinins with the anti-I specificity gave different banding patterns; this might be caused by the fact that they are directed against different parts of the I antigen.