High-performance hydrophobic interaction chromatography of proteins on reversed-phase supports coated with non-ionic surfactants of polyoxyethylene type Purification of a fungal aspartic proteinase

doi:10.1016/0021-9673(92)85046-V

Journal of Chromatography A

Volume 598, Issue 2, 15 May 1992, Pages 181-187

https://doi.org/10.1016/0021-9673(92)85046-V Get rights and content

Abstract

On coating reversed-phase supports with polyoxyethyelene-type non-ionic surfactants, proteins are no longer retained on such supports at moderate or low ionic strength, but they are retained at high ionic strength and can be desorbed by a decreasing ionic strength gradient. These reversibly modified supports were used for hydrophobic interaction chromatography (HIC). The proteins probably interact with the polyoxyethylene tail of the non-ionic surfactant while the hydrophobic part of the surfactant anchors the surfactant to the reversed-phase support by interactions with its alkane coverage. Although the interactions between non-ionic surfactant and reversed-phase support are non-covalent and the HIC mobile phases contained no surfactant, the modified columns were stable and could be used repeatedly. A surfactant-modified reversed-phase column provided a rapid, efficient, one-step purification of a fungal aspartic proteinase from a commercial crude preparation.

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¹: Present address: INSERM U 76, INTS, 6 Rue Alexandre Cabanel, 75739 Paris Cedex 15, France.

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High-performance hydrophobic interaction chromatography of proteins on reversed-phase supports coated with non-ionic surfactants of polyoxyethylene type Purification of a fungal aspartic proteinase

Abstract

Methods Enzymol.

J. Chromatogr.

J. Chromatogr.

J. Chromatogr.

J. Chromatogr.

J. Chromatogr.

Anal. Biochem.

J. Chromatogr.

Anal. Biochem.

J. Chromatogr.

J. Chromatogr.

J. Chromatogr.

J. Chromatogr.

Anal. Biochem.

J. Chromatogr.

J. Chromatogr.