Hydrophobic interaction chromatography of proteins

Xie, S., Svec, F., and Frechet, J.M.J., Rigid porous polyacrylamide-based monolithic columns containing butyl methacrylate as a separation medium for the rapid hydrophobic interaction chromatography of proteins,. Chromatogr. A, 775, 65, 1997. 

M.T.W. Hearn, Reversed-phase and hydrophobic interaction chromatography of proteins and peptides, in HPLC of Biological Macromolecules, 2nd ed., K.M. Gooding and F. Regnier (Eds.), Marcel Dekker, New York, 2002, pp. 172-173. 

Module 3, Column and Mobile Phase Design (CMP). This is the core module for ECAT. It can currently specify i) analytical column and mobile phase constituents for reverse phase chromatography of common classes of organic molecules ii) reverse phase, ion exchange phase and hydrophobic interaction chromatography of proteins and peptides iii) a limited set of specialty classes of molecules best treated by straight phase chromatography (e.g., mono- and disaccharides). The rules for selection of the HPLC detector are under development within Module 3. Some of the rules for detector mobile phase compatibility are already encoded. A set of rules for detector selection is ready but not yet encoded. 

Miller, N.T. and Shieh, C.H., Preparative hydrophobic interaction chromatography of proteins using ether based chemically bonded phases, J. Liq. Chromatogr., 9, 3269, 1986. 

Figure 2.9 Hydrophobic-interaction chromatography of proteins. (A) Ammonium sulfate gradient from 2.16 to 0 M (B) ammonium sulfate and tetrabutylammonium bromide gradients from 2.16 to 0 M and from 0 to 10 mM, respectively (C) ammonium sulfate and tetrabutylammonium bromide gradients from 2.16 to 0 M and from 0 to 20 mM, respectively (D) ammonium sulfate and tetrabutylammonium bromide gradients from 2.16 to 0 M and from 0 to 40 mM, respectively. Chromatography conditions column, silica-bound polyether, 10 cm x 4.6 mm I.D. temperature, 25°C flow rate, 1 ml/min gradient, linear for 30 min background buffer, 50 mM phosphate, pH 6.5. Peaks a, cytochrome c b, ribonuclease A c, /3-lactoglobulin A d, lysozyme e, ovalbumin f, a-chymotrypsinogen A g, fetuin. (Reprinted from Ref. 45 with permission.)...

Hydrophobic Interaction Chromatography of Proteins, Nucleic Acids, and Cells on... 

Zeng CM, Liao J-L, Nakazato K, and Hjerten S. Hydrophobic-interaction chromatography of proteins on continuous beds derivatized with isopropyl groups. J. Chromatogr. A 1996 753 227-234. 

M. I. Aguilar and M. T. W. Hearn, Reversed-phase and hydrophobic-interaction chromatography of proteins. 

R. H. Ingraham, Hydrophobic interaction chromatography of proteins, in High-Performance Liquid Chromatography of Peptides and Proteins (C. T. Mant and R. S. Hodges, eds.), CRC Press, Boca Raton, FL, 1991, p. 425. A. J. Alpert, J. Chromatogr 359 85 (1986). 

Kleinmann, I., Plicka, J., Smidl, P. and Vins, I. 1994. Hydrophobic interaction chromatography of proteins on HEMA-based sorbents. Am. Lab. April, 34H-34L. 

Ingraham, R.H. Hydrophobic interaction chromatography of proteins. In High-Performance Liquid Chromatography 10. of Peptides and Proteins Mant, C.T., Hodges, R.S., Eds. ... 

Fausnaugh, J.L. Regnier, F.E. Solute and mobile phase contributions to retention in hydrophobic interaction chromatography of proteins. J. Chromatogr. 1986, 359, 131. Wetlaufer, D.B. Koenigbauer, M.R. Surfactant-mediated protein hydrophobic-interaction chromatography. J. Chromatogr. 1986, 359, 55. 

Reversed-Phase and Hydrophobic Interaction Chromatography of Proteins and Peptides... 

To BC, Lenhoff AM. Hydrophobic interaction chromatography of proteins, II. Solution thermodynamic properties as a determinant of retention. J Chromatogr A 2007 1141(2) 235-43. 

Hjerten S. Hydrophobic interaction chromatography of proteins, nucleic acids, viruses, and cells on noncharged amphiphilic gels. Methods Biochem. Anal. 1981 27 89-108. 

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