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Suck, K; Walter, J; Menzel, F; Tappe, A; Kasper, C; Naumann, C; Zeidler, R; Scheper, T.
(2006): Fast and efficient protein purification using membrane adsorber systems.
J Biotechnol. 2006; 121(3):361-367 FullText FullText_BOKU

Abstract:
The purification of proteins from complex cell culture samples is an essential step in proteomic research. Traditional chromatographic methods often require several steps resulting in time consuming and costly procedures. In contrast, protein purification via membrane adsorbers offers the advantage of fast and gentle but still effective isolation. In this work, we present a new method for purification of proteins from crude cell extracts via membrane adsorber based devices. This isolation procedure utilises the membranes favourable pore structure allowing high flow rates without causing high back pressure. Therefore, shear stress to fragile structures is avoided. In addition, mass transfer takes place through convection rather than diffusion, thus allowing very rapid separation processes. Based on this membrane adsorber technology the separation of two model proteins, human serum albumin (HSA) and immungluboline G (IgG) is shown. The isolation of human growth hormone (hGH) from chinese hamster ovary (CHO) cell culture supernatant was performed using a cation exchange membrane. The isolation of the enzyme penicillin acylase from the crude Escherichia coli supernatant was achieved using an anion exchange spin column within one step at a considerable purity. In summary, the membrane adsorber devices have proven to be suitable tools for the purification of proteins from different complex cell culture samples. (c) 2005 Elsevier B.V. All rights reserved.
Authors BOKU Wien:
Almeria Ciarra
Kasper Cornelia
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Adsorption -
Animals -
CHO Cells -
Chromatography, Ion Exchange - methods
Cricetinae -
Culture Media, Conditioned - chemistry
Electrophoresis -
Enzyme-Linked Immunosorbent Assay -
Escherichia coli - enzymology
Growth Hormone - isolation & purification
Humans -
Hydrogen-Ion Concentration -
Membranes, Artificial -
Molecular Weight -
Penicillin Amidase - analysis
Proteins - isolation & purification
Serum Albumin - chemistry



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