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Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
Published on: January 8, 2014
Fast and efficient protein purification using membrane adsorber systems
Kirstin Suck1, Johanna Walter, Frauke Menzel
1Institut für Technische Chemie der Universität Hannover, Callinstrasse 3, D-30167 Hannover, Germany.
Journal of Biotechnology
|September 15, 2005
Summary
This study introduces a new, rapid protein purification method using membrane adsorbers, significantly reducing time and cost compared to traditional chromatography for proteomic research.
Area of Science:
- Biochemistry
- Proteomics
- Biotechnology
Background:
- Protein purification is crucial for proteomic research.
- Traditional chromatography is time-consuming and expensive.
- Membrane adsorbers offer a faster, gentler alternative.
Purpose of the Study:
- To present a novel method for protein purification from cell extracts using membrane adsorber devices.
- To demonstrate the efficiency and speed of this new technique.
Main Methods:
- Utilized membrane adsorber devices with favorable pore structures for high flow rates and low back pressure.
- Employed convective mass transfer for rapid separation.
- Applied cation and anion exchange membrane adsorbers.
Main Results:
- Successfully separated model proteins like human serum albumin (HSA) and immunoglobulin G (IgG).
- Isolated human growth hormone (hGH) from Chinese Hamster Ovary (CHO) cell culture supernatant.
- Purified penicillin acylase from Escherichia coli supernatant in a single step with high purity.
Conclusions:
- Membrane adsorber devices provide a fast, effective, and gentle method for protein purification.
- This technology is suitable for various complex cell culture samples.
- Offers a significant improvement over conventional chromatographic techniques.
