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Hydrophobic chromatography of β‐galactosidase

Hydrophobic chromatography of β‐galactosidase 10.1002/bit.260220211.abs The hydrophobic interaction of β‐galactosidase with Sepharose 4B substituted with 3,3′‐diaminodipropylamine was studied in both batch and column experiments. The equilibrium and the binding rate constants were determined for different phosphate buffer concentrations. The equilibrium constants exhibit a hysteresis effect, i.e., desorption constants are less than adsorption constants, and the higher the ionic strength to start the desorption, the larger the effect. The rate data are not satisfactorily described by a simple reversible first‐order model. The column chromatographic data are semiquantitatively described by a local equilibrium theory without axial dispersion or intraparticle diffusion. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology and Bioengineering Wiley

Hydrophobic chromatography of β‐galactosidase

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References (20)

Publisher
Wiley
Copyright
Copyright © 1980 John Wiley & Sons, Inc.
ISSN
0006-3592
eISSN
1097-0290
DOI
10.1002/bit.260220211
pmid
6766333
Publisher site
See Article on Publisher Site

Abstract

10.1002/bit.260220211.abs The hydrophobic interaction of β‐galactosidase with Sepharose 4B substituted with 3,3′‐diaminodipropylamine was studied in both batch and column experiments. The equilibrium and the binding rate constants were determined for different phosphate buffer concentrations. The equilibrium constants exhibit a hysteresis effect, i.e., desorption constants are less than adsorption constants, and the higher the ionic strength to start the desorption, the larger the effect. The rate data are not satisfactorily described by a simple reversible first‐order model. The column chromatographic data are semiquantitatively described by a local equilibrium theory without axial dispersion or intraparticle diffusion.

Journal

Biotechnology and BioengineeringWiley

Published: Feb 1, 1980

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