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G. Craven, E. Steers, C. Anfinsen (1965)
PURIFICATION, COMPOSITION, AND MOLECULAR WEIGHT OF THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12.The Journal of biological chemistry, 240
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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.
Biotechnology and Bioengineering – Wiley
Published: Feb 1, 1980
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