Separation of amphipathic proteins based on adsorption to hexadecane: Water interfaces

Mel Rosenberg; Naomi Regimov; Ilana Eli; Mel Rosenberg; Zinaida Zosim

doi:10.1080/10826068608062275

Separation of amphipathic proteins based on adsorption to hexadecane: Water interfaces

Mel Rosenberg, Naomi Regimov, Ilana Eli, Mel Rosenberg, Zinaida Zosim

Tel Aviv University

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

A method is proposed for the relatively simple and rapid separation of amphipathic biopolymers, based on adsorption onto and desorption from the surface of hexadecane droplets. Adsorption to the hexadecane:water interface was carried out by mixing hexadecane with aqueous protein solutions at room temperature. Desorption was performed by consecutive solidification and melting of the liquid hydrocarbon (m.p. 18° C), resulting in coalescence of the droplets and reappearance of the desorbed moiety in the bulk aqueous phase. Of interest was the observation that lysozyme remains enzymatically active following this procedue.

Original language	English
Pages (from-to)	133-141
Number of pages	9
Journal	Preparative Biochemistry
Volume	16
Issue number	2
DOIs	https://doi.org/10.1080/10826068608062275
State	Published - 1 Jun 1986

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abstract = "A method is proposed for the relatively simple and rapid separation of amphipathic biopolymers, based on adsorption onto and desorption from the surface of hexadecane droplets. Adsorption to the hexadecane:water interface was carried out by mixing hexadecane with aqueous protein solutions at room temperature. Desorption was performed by consecutive solidification and melting of the liquid hydrocarbon (m.p. 18° C), resulting in coalescence of the droplets and reappearance of the desorbed moiety in the bulk aqueous phase. Of interest was the observation that lysozyme remains enzymatically active following this procedue.",

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AU - Rosenberg, Mel

AU - Regimov, Naomi

AU - Eli, Ilana

AU - Rosenberg, Mel

AU - Zosim, Zinaida

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Separation of amphipathic proteins based on adsorption to hexadecane: Water interfaces

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