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

Wilkinson, M L, Iqbal, M J, Forbes, A, Corbishley, T P and Williams, R (1986) 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. Biochemical Journal, 240 (1). pp. 75-9. ISSN 0264-6021

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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.

Item Type: Article
Uncontrolled 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
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
Depositing User: Pure Connector
Date Deposited: 06 Aug 2014 11:58
Last Modified: 11 Apr 2019 15:39
URI: https://ueaeprints.uea.ac.uk/id/eprint/49498
DOI:

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