An Improved Method for the Purification of Rat Serum Albumin: Removal of Contaminants by Concanavalin A-Sepharose1
- 1 May 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 81 (5) , 1293-1297
- https://doi.org/10.1093/oxfordjournals.jbchem.a131582
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 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.This publication has 4 references indexed in Scilit:
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