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Application of oestrogen receptor ligand binding domain to the generic isolation of oestrogens by receptor affinity chromatography

Byford, M.F.; Sauer, M.J.

Chromatographia 59(Supp): S123-S130

2004


ISSN/ISBN: 0009-5893
DOI: 10.1365/s10337-003-0246-4
Accession: 004045677

Human oestrogen receptor (alpha) ligand binding domain (hER-LBD) was expressed in E. coli and isolated using a novel approach. The solubilized recombinant receptor had the expected biological activity in terms of ligand binding affinity and selectivity, indicating the potential for use in the proposed receptor affinity chromatography (RAC) application.

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