Expression and Purification of Recombinant Rabbit and Human Phosphoglucomutase
Inventors: John Markley, Ronnie Frederick, Young Kee Chae
The Wisconsin Alumni Research Foundation (WARF) is seeking commercial partners interested in developing a method for expressing and purifying phosphoglucomutase (PGM) using an E. coli system.
Phosphoglucomutase (PGM) is a glycolytic enzyme that converts glucose 1-phosphate to glucose 6-phosphate. This enzyme plays a major role in directing the flow of carbon toward either anabolic or catabolic pathways. Purified PGM is very unstable – it precipitates in an inactive form when frozen and retains activity when refrigerated for only a few days. As a result, PGM requires frequent re-isolation and is difficult to obtain in large quantities.
UW-Madison researchers have now developed a method for expressing and purifying PGM using an E. coli system. Their technique produces high yields of recombinant PGM in a soluble, active form. A variety of materials are available for licensing, including whole cell pastes of recombinant E. coli, cell-free extracts and purified recombinant proteins.
- Production of PGM
- Provides higher yields of soluble, active PGM enzyme than previous methods
- System has successfully produced both recombinant rabbit muscle and human PGM.