Assessment of the purification of a protein by ion exchange and gel permeation chromatography
Article first published online: 3 NOV 2006
Copyright © 2002 International Union of Biochemistry and Molecular Biology, Inc.
Biochemistry and Molecular Biology Education
Volume 30, Issue 3, pages 179–183, May 2002
How to Cite
Pugh, M. E. and Schultz, E. (2002), Assessment of the purification of a protein by ion exchange and gel permeation chromatography. Biochem. Mol. Biol. Educ., 30: 179–183. doi: 10.1002/bmb.2002.494030030029
- Issue published online: 3 NOV 2006
- Article first published online: 3 NOV 2006
- Manuscript Received: 14 DEC 2001
A 3-week group laboratory project experiment that involves the partial purification of myoglobin (Mb) from bovine hamburger is described. The experiment compares alternate purification methods (gel filtration and ion exchange chromatography) as to both overall yield and enhancement in relative purity. The purity and molecular weight of purified Mb is established by SDS-PAGE. Group reports are directed toward having students put together all the information that is collected in the experiment. We discuss what we have learned and continue to learn from experiments done in the cooperative learning mode.