A three-step purification of human alpha 1-acid glycoprotein.
alpha 1-Acid glycoprotein (AGP) was purified to homogeneity by a 3-step procedure using pseudo-ligand affinity chromatography on immobilized Cibacron blue F3GA, Procion red HE3B, and preparative column isoelectric focusing. The overall yield of the combined techniques was 88%. Analysis of the purified AGP by lectin affinity chromatography on immobilized Con A and immunoaffino-electrophoresis indicated that the most acidic form did not interact with the lectin, while the two more basic fractions possessed different affinities for Con A. In addition, 3 different populations of AGP were clearly separated by Con A affinity chromatography.
D002846:Chromatography, Affinity / Q000379:methods; D004396:Coloring Agents; D003208:Concanavalin A; D006801:Humans; D007122:Immunoelectrophoresis; D007525:Isoelectric Focusing / Q000379:methods; D009961:Orosomucoid / Q000302:isolation & purification*; D014227:Triazines
D004396:Coloring Agents; D009961:Orosomucoid; D014227:Triazines; D003208:Concanavalin A; C012842:Cibacron Blue F 3GA; C020795:procion red HE-3B