A three-step purification of human alpha 1-acid glycoprotein |
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| Authors: | P Laurent L Miribel J Bienvenu C Vallve P Arnaud |
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| Affiliation: | 1. Department of Immunology, Pasteur Institute of Lyon, 77 rue Pasteur, 69365 Lyon Cédex 02, France;2. Department of Basic and Clinical Immunology and Microbiology, Medical University of South Carolina, Charleston, SC 29425, USA |
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| Abstract: | 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. |
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| Keywords: | Orosomucoid Cibacron blue Procion red Preparative isoelectric focusing |
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