English  |  正體中文  |  简体中文  |  Items with full text/Total items : 43312/67235
Visitors : 2169418      Online Users : 18
RC Version 5.0 © Powered By DSPACE, MIT. Enhanced by NTU/NCHU Library IR team.
National Chung Hsing University Institutional Repository - NCHUIR > 工學院 > 化學工程學系所 > 依資料類型分類 > 期刊論文 >  Adsorption behaviors of recombinant proteins on hydroxyapatite-based immobilized metal affinity chromatographic adsorbents

Please use this identifier to cite or link to this item: http://nchuir.lib.nchu.edu.tw/handle/309270000/128962

標題: Adsorption behaviors of recombinant proteins on hydroxyapatite-based immobilized metal affinity chromatographic adsorbents
作者: Lin, P.C.;Lin, S.C.;Hsu, W.H.
關鍵字: IMAC;adsorption isotherm;protein purification;d-glucosamine 2-epimerase;substrate-specificity;varying particle;structural basis;purification;acid;resolution;peptides;binding;ions
日期: 2008
Issue Date: 2012-12-07 15:16:46 (UTC+8)
關連: Journal of the Chinese Institute of Chemical Engineers, Volume 39, Issue 5, Page(s) 389-398.
摘要: The equilibrium adsorption of three homo-oligoemric model recombinant proteins containing up to 8 poly(histidine) affinity tags on a hydroxyapatite-based immobilized metal affinity chromatography (IMAC) adsrobernt is reported in this study. The experimental data are well fitted with the three-parameter Langmuir-Freudlich isotherm model, indicating the presencce of positive cooperativity for the adsorption of these model proteins. The maximum capacity and the binding affinity of the IMAC adsorbent for the model proteins are in principle dependent on the size and the number of affinity tags of proteins, respectively. The exceptionally high association constant of the octameric racemase, probably due to simultaneous multipoint attachment, make it difficult to elute racemase from the adsorbent. The adsoption isotherms under denaturing conditions are well fitted with the Langmuir model. Result of Scatchard analysis further suggest the homogeneous adsorption of the model proteins subunits under denaturing conditions. The binding capacitites and affinities of the adsorbent under denaturing conditions for the three unfolded protein subunits become essentially identical because the molecular size and number of polu(His) tags of the unfolded polypeptide chains of the three protein subunits are the same. The significant reduction in association constants under denaturing conditions suggests that high concentration of urea could interfere with the binding of proteins on the hydroxyapatite-based adsorbent. (c) 2008 Taiwan Institute of Chemical Engineers, Published by Elsevier B.V. All rights reserved.
Relation: Journal of the Chinese Institute of Chemical Engineers
Appears in Collections:[Category+by+Data+Type] Journal Articles
[Category+by+Professor] Sung-Chyr Lin

loading Web of Knowledge data....

Files in This Item:

File SizeFormat






聯絡網站維護人員:wyhuang@nchu.edu.tw,04-22840290 # 412。

DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU/NCHU Library IR team Copyright ©   - Feedback