Purification of Erythropoietin by Ion-Exchange Chromatography.

Abstract

A method for purification of erythropoietin from the filtrate of acidified, boiled plasma prepared from phenylhydrazine anemic rabbits utilizing DEAE-cellulose ionexchange columns has been described. The active erythropoietic factor thus prepared has been partially characterized and shown to be a low molecular weight, acidic glycoprotein.