Abstract
Minor contaminants occasionally found in conventionally prepared rat serum albumin were easily and completely removed by concanavalin A-Sepharose chromatography. The unad-sorbed fraction from a concanavalin A-Sepharose column contained albumin which was homo-geneous on polyacrylamide gel electrophoresis. The recovery of albumin from 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 α-methyl-D-glucoside from the concanavalin A-Sepharose column, and resolved into three components by gel electrophoresis. There was one major glycoprotein, possibly α1-antitrypsin, and two minor proteins one of which was albumin.
