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Preparation of molecular imprinted polymer with quaternary ammonium groups as recognition sites for separation of pig cyclophilin 18 and bovine serum albumin
Author(s) -
Liu Huijuan,
Han Ruifang,
Feng Miao,
Gao Junfei,
Long Yi,
Zhao Zhuo,
Wang Ying,
Mi Huaifeng
Publication year - 2010
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.201000038
Subject(s) - cationic polymerization , bovine serum albumin , chemistry , polymer , adsorption , molecular recognition , molecularly imprinted polymer , polymerization , protein purification , selective adsorption , ammonium , protein adsorption , chromatography , template , polymer chemistry , combinatorial chemistry , selectivity , molecule , organic chemistry , materials science , nanotechnology , catalysis
Abstract We introduce a new type of molecular imprinted polymer (MIP) with immobilized assistant recognition polymer chains (ARPCs) to create effective recognition sites. In this work, cloned pig cyclophilin 18 (pCyP18) and BSA were used as templates, respectively. The template protein was selectively assembled with ARPCs from the library which consists of numerous limited length polymer chains with randomly distributed recognition sites of the quaternary ammonium cationic groups and immobilizing sites. The assemblies of protein and ARPCs were adsorbed by macroporous microspheres and immobilized by cross‐linking polymerization. After removing the templates, the two kinds of synthesized MIPs were used to adsorb cloned pCyP18 and BSA from protein mixtures respectively and both showed high selectivity. It confirms that this new method is suitable to separate proteins of both low and high molecular weight. The extended experiment on adsorption of natural pCyP18 from cytosol shows that the obtained MIP using cloned protein as template can be used to enrich natural protein of low content.