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J. Biochem, 1977, Vol. 81, No. 5 1293-1297
© 1977 Japanese Biochemical Society

research-article

An Improved Method for the Purification of Rat Serum Albumin: Removal of Contaminants by Concanavalin A-Sepharose1

Yukio IKEHARA, Kimimitsu ODA and Keitaro KATO

Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyushu University Fukuoka 812

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 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 {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.

1This work was supported in part by a grant from the Ministry of Education, Science and Culture of Japan.


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