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Digitale Medien

Hydrophobic chromatography of β-galactosidase (1980)

Chang, C.-T. ; McCoy, B. J. ; Carbonell, R. G.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 22 (1980), S. 377-399

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Details

ISSN: 0006-3592

Schlagwort(e): Chemistry ; Biochemistry and Biotechnology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung

Notizen: 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.

Zusätzliches Material: 11 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/bit.260220211

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