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

M L Wilkinson, M J Iqbal, A Forbes, T P Corbishley, R Williams

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Abstract

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.
Original languageEnglish
Pages (from-to)75-9
Number of pages5
JournalBiochemical Journal
Volume240
Issue number1
Publication statusPublished - 15 Nov 1986

Keywords

  • Androstane-3,17-diol
  • Carrier Proteins
  • Chromatography, Affinity
  • Enzyme-Linked Immunosorbent Assay
  • Female
  • Fetal Proteins
  • Humans
  • Hydrogen-Ion Concentration
  • Ligands
  • Molecular Weight
  • Pregnancy
  • Sex Hormone-Binding Globulin

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