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Updated: Sep 28, 2026

Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
Published on: January 8, 2014
Purification of human immunoglobulin G: a new approach to plasma fractionation
Background And Objectives:
Currently, plasma fractionation involves multiple processing steps using established methods such as ethanol precipitation and column chromatography. The known limitations associated with conventional purification techniques, combined with strict regulations on safety and high demand for particular plasma proteins, have resulted in a shortage of plasma-derived therapeutics such as intravenous immunoglobulin G (IgG).
Materials And Methods:
In this study, IgG was purified from human plasma using Gradiflow technology, an electrophoresis-based separation technology.
Results:
IgG was isolated from plasma to high purity, with 94 +/- 5% recovery in a short processing time.
Conclusions:
The technology has been shown to be linearly scalable and has the capacity to contribute to increased production of important plasma fraction therapeutics.
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