Assessment of the purification of a protein by ion exchange and gel permeation chromatography

Abstract

AbstractA 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.