Determination of a glycosyl subunit of human serum albumin by concanavalin A-sepharose.
A new procedure has been devised for the isolation of a glycosyl subunit of albumin from human serum. After the selective removal from serum proteins with affinity chromatography on Blue-Sepharose CL-6B, albumin was applied to a column of concanavalin-A Sepharose which resolved the protein in two subunits with different specific colour activity for carbohydrates, as tested with thiobarbituric acid assay. The glycosyl albumin bound to concanavalin-A Sepharose was homogeneous when examined by immunoelectrophoresis and sodium dodecyl-sulphate polyacrylamide electrophoresis, whereas it showed a microheterogeneity when tested by isoelectric focusing. The procedure was applied to a model system as well as to serum from normal and diabetic patients.
D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography / Q000379:methods; D003920:Diabetes Mellitus / Q000097:blood; D004591:Electrophoresis, Polyacrylamide Gel; D017127:Glycation End Products, Advanced; D006801:Humans; D007122:Immunoelectrophoresis; D007525:Isoelectric Focusing; D012685:Sepharose / Q000031:analogs & derivatives; D012709:Serum Albumin; D000093423:Glycated Serum Albumin
D002241:Carbohydrates; D017127:Glycation End Products, Advanced; D012709:Serum Albumin; C028326:concanavalin A-sepharose; D012685:Sepharose; D000093423:Glycated Serum Albumin