Abstract
Plasmin degrades gammaG-globulin very similarly to trypsin. Plasmin degrades the polymers in gamma-globulin preparations, but it simultaneously fragments the monomer gamma- globulin even in low concentration. Therefore it is not ideal for the preparation of a polymer free gamma-globulin that does not fix complement. By gel filtration through Sephadex G-200, the aggregates are separated from the mono-mer 7 S gamma-globulin which is not anticomplementary. This mono-mer fraction soon gives rise to new C[image]-fixing di- and polymers of the gammaG- globulin.