Related Experiment Videos
A convenient method for affinity purification of maltose binding protein fusions
1Department of Chemistry, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Journal of Biotechnology
|September 8, 1998
Summary
Maltose binding protein fusions from Escherichia coli can be purified using a simple cellulose and starch mixture. This method offers an effective alternative to complex media for affinity chromatography.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Engineering
Background:
- Maltose binding protein (MBP) from Escherichia coli is a widely used fusion partner in protein biosynthesis.
- Its utility stems from the ease of affinity purification of MBP fusion proteins.
Purpose of the Study:
- To identify a simpler and effective medium for affinity purification of MBP fusions.
- To provide an alternative to currently used complex chromatographic media.
Main Methods:
- Utilized a mixture of cellulose and starch as a novel medium for affinity chromatography.
- Applied this medium for the purification of MBP fusions.
Main Results:
- A cellulose and starch mixture proved to be a simple and effective medium for MBP fusion purification.
- This approach bypasses the need for more complicated and expensive purification media.
Conclusions:
- Cellulose and starch offer a cost-effective and straightforward method for purifying MBP fusion proteins.
- This finding simplifies a common practice in protein biotechnology and research.