Affinity chromatography of rat alpha-fetoprotein on estradiol-agarose columns.

The use of 17 beta-estradiol-17-hemisuccinate coupled to agarose beads is shown to be a rapid and simple procedure for the isolation of alpha-fetoprotein (AFP) from amniotic fluid. The elution profile of the affinity column shows that AFP is sufficiently retarded by the gel to perform the purification of the protein without specific elution with high-affinity AFP ligands. Rat AFP appeared as a single symmetric peak, a profile that is in good agreement with the existence of a single population of AFP molecules having estrogen-binding properties.