Alpha -1-antitrypsin is the main protease inhibitor in human serum. Certain variants or phenotypes of this protein are associated with diseases of the liver and lung. The availability of purified alpha-1-antitrypsin of various phenotypes would be useful in studies exploring these associations. A two-step purification procedure is presented which involves affinity chromatography on isolubilized conconavalin A followed by preparative starch gel electrophoresis. This simple and rapid method has provided both MM and ZZ alpha-1-antitrypsin in highly pure and active form.