THERMODYNAMIC MODEL FOR ELECTROSTATIC-INTERACTION CHROMATOGRAPHY OF PROTEINS

被引：29

作者：

MAZSAROFF, I

VARADY, L

MOUCHAWAR, GA

REGNIER, FE

机构：

[1] PURDUE UNIV,DEPT BIOCHEM,W LAFAYETTE,IN 47907

[2] PURDUE UNIV,DEPT ELECT ENGN,W LAFAYETTE,IN 47907

来源：

JOURNAL OF CHROMATOGRAPHY | 1990年 / 499卷

关键词：

D O I：

10.1016/S0021-9673(00)96964-4

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

A thermodynamic model derived by Record et al. [M. T. Record, Jr., Biopolymers, 14 (1975) 2137 and M. T. Record, Jr., C. F. Anderson and T. M. Lohman, Q. Rev. Biophys., 11 (1978) 103] from Wyman's linkage theory [J. Wyman, Adv. Protein Chem., 19 (1964) 223] using Manning's condensation model [J. Manning, J. Chem. Phys., 51 (1969) 924] was extended to electrostatic interaction chromatography. Mixed, electrostatic and hydrophobic interactions of a model protein, ovalbumin were characterized by ion and water release. © 1990.

引用

页码：63 / 77

页数：15

共 38 条

[1]

ALPERT A, 1979, J CHROMATOGR, V158, P375

[2] NA-23 NMR-STUDIES OF CATION DNA INTERACTIONS [J].