Expression, purification, and binding properties of human cellular retinoic acid-binding protein type I and type II.

Abstract

Human cellular retinoic acid-binding protein (CRABP) type I and type II were expressed in Escherichia coli from cloned cDNAs. Expressed proteins were purified by gel filtration and ion-exchange chromatography, resulting in highly pure proteins. The yield after gel filtration was approximately 50 mg/liter bacterial culture. In binding studies the equilibrium… (More)

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@article{Fogh1993ExpressionPA, title={Expression, purification, and binding properties of human cellular retinoic acid-binding protein type I and type II.}, author={Karsten Fogh and John J . Voorhees and Anders {\AA}str{\"{o}m}, journal={Archives of biochemistry and biophysics}, year={1993}, volume={300 2}, pages={751-5} }