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 ORCID: https://orcid.org/0000-0001-7416-9843, 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
UEA Research Groups:	Faculty of Medicine and Health Sciences > Research Groups > Gastroenterology and Gut Biology Faculty of Medicine and Health Sciences > Research Groups > Nutrition and Preventive Medicine
Depositing User:	Pure Connector
Date Deposited:	06 Aug 2014 10:58
Last Modified:	24 Oct 2022 23:58
URI:	https://ueaeprints.uea.ac.uk/id/eprint/49498
DOI:

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