A three‐step purification of human α1‐acid glycoprotein
- 12 March 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 168 (1) , 79-83
- https://doi.org/10.1016/0014-5793(84)80210-0
Abstract
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.Keywords
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