[Comparative analysis of gamma globulin preparations isolated by means of DEAE-Sephadex and DEAE-cellulose].

Preparations of rabbit gamma-globulin obtained with the aid of ion-exchange chromatography on DEAE-Sephadex contained an admixture of other serum proteins revealed by disc-electrophoresis in acrylamide gel. This impurity can be eliminated by rechromatography of gamma-globulin preparations of DEAE-cellulose in the same buffer solutions which were used for purification of gamma-globulin on DEAE-Sephadex. Better purification of gamma-globulin on DEAE-cellulose can supposedly be attributed to the effective absorption on cellulose basis of euglobulin aggregates which form in the solutions with a low ionic power used for chromatographic isolation of gamma-globulin on ion-exchangers.