By Michael Heidelberger
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Additional resources for Lectures in Immunochemistry
One can add a dilute solution of Type I capsular polysaccharide instead of the cells and this also combines chemically with the excess antibody on the bacterial cells and brings about a reagglutination into very much larger particles through links with the soluble molecules of polysaccharide. This also shows that the reaction is due to the polysaccharide on the surface of the cells added, for it makes no difference whether one adds it in solution or on the cell surface: one gets the same effect of reagglutination.
R. C. Krueger and I repeated this work with several horse antisera. W e did not know about Dr. Oikawa's work until after we had done our own. W e found that not only did one get at least as much nitrogen out after complete removal of the lipids with alcohol and ether under conditions such that the protein was not extensively denatured, but one actually got more precipitate. The reason probably is that in the horse antisera, as we noted before, the antibodies are very large molecules in the water-insoluble group of globulins.
The lower curve is of some interest because it represents a type of cross reaction which one gets between very closely related proteins. S... Α *" Α. ' \ / Α. Α ' Α.  Fig. 3 . Two-dimensional representation of specific precipitates: [ 1 ] S-anti-S; [ 2 ] Ea-anti-Ea. S = specific polysaccharide, Ea = crystalline egg albumin, A = antibody. egg albumin, E a c . About 60 per cent of the antibody nitrogen is precipitated at the maximum and the characteristics of the reaction are almost the same as of the homologous one.