A three‐step purification of human α1‐acid glycoprotein

FEBS Letters

Arnaud, Philippe¹  Bienvenu, Jacques²  Miribel, Laurent²  Vallve, Charles²  Laurent, Philippe² 

[1]Department of Basic and Clinical Immunology and Microbiology, Medical University of South Carolina, Charleston, SC 29425, USA

[2]Department of Immunology, Pasteur Institute of Lyon, 77 rue Pasteur, 69365 Lyon Cédex 02, France

关键词: α1-Acid glycoprotein;    Orosomucoid;    Cibacron blue;    Procion red;    Preparative isoelectric focusing;   

DOI  :  10.1016/0014-5793(84)80210-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α₁-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 immunoaffinoelectrophoresis 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.

【 授权许可】

Unknown