[Studies of chromatographic behaviors of proteins on synthesized cation-exchanger].
A chelating weak cation-exchanger has been synthesized by indirect method using domestic materials. The chromatographic performance of the synthesized packing was studied in detail, and compared with separation efficiency of commercial columns (Shim-Pack WCX-1 and Poly CATA). The chromatographic thermodynamics of proteins in weak cation-exchange system was studied over a wide temperature range. The thermodynamic parameters (deltaH0 and deltaS0) and the compensation temperature (beta) at protein denaturation were determined by their chromatographic thermal behaviors. By using the obtained standard entropy change (deltaS0), the conformational change of proteins can be judged. The compensation relationship between deltaH0 and deltaS0 was used to identify the identity of individual protein retention mechanism in chromatographic system. The interaction between chelating weak cation-exchanger and metal ions was examined. The retention mechanism of protein in metal chelating chromatography was explored.
Li
Rong
R
School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710049, China. chengjingze@yahoo.com
Chen
Guoliang
G
Zhao
Wenming
W
D002411:Cation Exchange Resins / Q000138:chemical synthesis / Q000737:chemistry*; D002614:Chelating Agents / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D002852:Chromatography, Ion Exchange / Q000379:methods*; D006801:Humans; D011489:Protein Denaturation; D011506:Proteins / Q000032:analysis* / Q000737:chemistry; D013816:Thermodynamics
D002411:Cation Exchange Resins; D002614:Chelating Agents; D011506:Proteins