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Updated: Apr 30, 2026

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Published on: June 19, 2012

Separation and identification of different refolding components.

Ming Li¹, Zhiguo Su

¹National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100080, PR China.

Journal of Biotechnology

|June 20, 2003

Summary

This summary is machine-generated.

High-concentration lysozyme refolding was achieved using dual-gradient ion-exchange chromatography. Subsequent size-exclusion chromatography separated refolding components, aiding in understanding protein renaturation dynamics.

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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Published on: December 12, 2017

Area of Science:

Biochemistry
Protein Chemistry
Chromatography

Background:

Protein misfolding and aggregation are significant challenges in biotechnology.
Efficient refolding of proteins at high concentrations is crucial for industrial applications.
Ion-exchange chromatography (IEC) is a common technique for protein purification and refolding.

Purpose of the Study:

To develop and optimize a dual-gradient ion-exchange chromatography (IEC) method for high-concentration protein refolding.
To characterize the separated components resulting from the refolding process.
To investigate the hydrodynamic and hydrophobic properties of these components.

Main Methods:

Dual-gradient ion-exchange chromatography (IEC) was employed for lysozyme refolding.
Size-exclusion chromatography (SEC) was used to separate refolding intermediates and products.
Low concentrations of urea and NaCl were added to the SEC elution buffer.
Hydrodynamic characteristics and hydrophobic properties of separated components were analyzed.

Main Results:

Successful renaturation of lysozyme at high concentrations was demonstrated using the developed IEC method.
SEC effectively separated different refolding components, including soluble and aggregated forms.
Analysis revealed distinct hydrodynamic and hydrophobic profiles for the separated species.

Conclusions:

Dual-gradient IEC is an effective strategy for high-concentration protein refolding.
SEC coupled with buffer additives provides a means to analyze complex refolding mixtures.
Understanding component characteristics aids in optimizing protein refolding protocols.