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https://hdl.handle.net/2440/92671
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Type: | Journal article |
Title: | Tris(hydroxymethyl)aminomethane-functionalized agarose particles: parameters affecting the binding of bovine serum albumin |
Author: | Zhang, B. Wang, Y. Gao, M. Gu, M. Wang, C. |
Citation: | Journal of Separation Science, 2012; 35(12):1406-1410 |
Publisher: | Wiley-VCH Verlag |
Issue Date: | 2012 |
ISSN: | 1615-9306 1615-9314 |
Statement of Responsibility: | Bin Zhang, Ye Wang, Min Gao, Ming Gu, and Changhai Wang |
Abstract: | A new protein adsorbent is introduced based on the coupling of the common buffer ion, tris(hydroxymethyl)aminomethane, to the agarose gel Sepharose HPfrom GEHealthcare Bio-Sciences AB, Uppsala, Sweden. The article describes the synthesis of the new adsorbent and the use of BSA as a model in a binding study. By optimization of the coupling procedure, a maximum ligand density of 63.5 μmol/mL gel could be obtained. Adsorption equilibria were investigated in the pH range 5.0–8.0 and at salt concentrations of 0–0.4 mol/L. Binding of BSA under different conditions indicated that both electrostatic interaction and hydrogen bonding were involved in the adsorption process where the former played a major role. |
Keywords: | Adsorption equilibrium; Bovine serum albumin; Protein adsorption; Sepharose HP; Tris(hydroxymethyl)aminomethane |
Rights: | © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim |
DOI: | 10.1002/jssc.201200118 |
Published version: | http://dx.doi.org/10.1002/jssc.201200118 |
Appears in Collections: | Aurora harvest 7 Chemical Engineering publications |
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