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Ligand binding properties of human cellular retinoic acid binding protein II expressed in E. coli as a glutathione-S-transferase fusion protein

Lookup NU author(s): Dr Chris Redfern, Kate Wilson

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Abstract

To test the hypothesis that 9-cis-retinoic acid is a ligand for cellular retinoic acid binding protein II (CRABP II), human CRABP II was expressed as a glutathione-S-transferase fusion protein (GST-CRABP II) and a single affinity purification step used to extract it from bacterial lysates. GST-CRABP II bound all trans-retinoic acid with high affinity (K(d) 14.2 +/- 6.5 nM), but 9-cis-retinoic acid bound poorly. These studies suggest that 9-cis-retinoic acid is not a ligand for CRABP II. Their ease of purification makes GST-CRABP fusion proteins useful tools for ligand binding studies with different retinoids.


Publication metadata

Author(s): Redfern CPF, Wilson KE

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 1993

Volume: 321

Issue: 2-3

Pages: 163-168

Print publication date: 01/04/1993

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

URL: http://dx.doi.org/10.1016/0014-5793(93)80100-9

DOI: 10.1016/0014-5793(93)80100-9


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