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In order to develop an immunoassay for foetal steroid-binding protein in human serum, which is impossible to assay quantitatively in normal samples by conventional ligand-binding techniques, the protein was purified by salt precipitation, affinity chromatography and gel filtration. Elution was by competing ligand or alkaline pH. The purified protein was further characterized and a highly specific antiserum was raised in rabbits.

biochemical journal

Purification of foetal steroid-binding protein from human serum by affinity chromatography on 5α-androstane-3 β,17 β-diol 3-hemisuccinate-aminohexyl-Sepharose 6B