High-performance liquid chromatography of proteins: purification of alpha-fetoprotein from fetal calf serum
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Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Journal of Chromatography
|September 14, 1984
Abstract:
High-performance liquid chromatography was utilized for the purification of bovine alpha-fetoprotein (BAFP) from fetal calf serum (FCS). An initial step in the purification involved absorption of charcoal delipidated FCS on Cibacron Blue F3GA gel. The Cibacron Blue pre-purified FCS was then chromatographed on a Polyanion SI weak anion-exchange column. The BAFP isolated had a purity of greater than 93% with an overall yield of 48% from FCS. The procedure was applicable for semi-preparative scale purification of BAFP.

