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High-performance liquid chromatography of amino acids, peptides and proteins : XCV. Thermodynamic and kinetic investigations on rigid and soft affinity gels with varying particle and pore sizes: Comparison of thermodynamic parameters and the adsorption behaviour of proteins evaluated from bath and frontal analysis experiments by F.B. Anspach; A. Johnston; H.-J. Wirth; K. K. Unger; M.T.W. Hearn is a Chemistry article available to read on EtoBox.

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The thermodynamic constants, associated with the interaction of three proteins with triazine dye affinity sorbents, have been derived from bath and frontal analysis experiments. In cases where mass-transfer restrictions are very high, calculation of the thermodynamic constants directly from frontal analysis experiments could not be achieved. In such cases, a portion of the adsorbate was always present in the effluent, a situation which has its effect as the split peak phenomenon. With Fractogel-based triazine dye affinity sorbents none of the test proteins applied in frontal analysis were adsorbed. A similar behaviour was observed for a Cellufine sorbent during the adsorption of human serum albumin and the Blue Sepharose CL6B sorbent during the adsorption of alcohol dehydrogenase, which displayed much slower apparent adsorption kinetics than observed in the bath experiments. These phenomena were shown to be associated with changes in the gel structure, caused in part by the column packing procedure. Silica-based sorbents performed better in the adsorption of lysozyme in the column mode than soft-gel affinity sorbents, as was evident in the higher capacities and steeper breakthrough

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Author

F.B. Anspach; A. Johnston; H.-J. Wirth; K. K. Unger; M.T.W. Hearn

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1873-3778)

Published

1990

Language

EN

Field

Chemistry (Physical Sciences)