title: An improved method for the purification of rat serum albumin: removal of contaminants by concanavalin A-Sepharose.
abstract: Minor contaminants occasionally found in conventionally prepared rat serum albumin were easily and completely removed by concanavalin A-Sepharose chromatography. The unadsorbed fraction from a concanavalin A-Sepharose column contained albumin which was homogeneous on polyacrylamide gel electrophoresis. The recovery of albumin form rat serum was approximately 30%. Approximately 2% of the added protein obtained as an albumin peak in DEAE-cellulose chromatography was adsorbed on and eluted with alpha-methyl-D-glucoside from the concanavalin A-Sepharose column, and resolved into three components by gel electrophoresis. There was one major glycoprotein, possibly alpha 1-antitrypsin, and two minor proteins one of which was albumin.
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D003208:Concanavalin A; D007122:Immunoelectrophoresis; D008722:Methods; D051381:Rats; D012685:Sepharose; D012709:Serum Albumin / Q000302:isolation & purification*
chemical_list: D012709:Serum Albumin; D003208:Concanavalin A; D012685:Sepharose