CHED 933 |
| Gp96 is a highly conserved and abundant endoplasmic reticulum (ER) chaperone protein that is upregulated in response to stress. It has been previously shown by our lab that gp96 undergoes spontaneous self assembly into high molecular weight complexes when exposed to temperatures as low as 42°C and that self assembly is inhibited by physiological concentrations of ATP. Through electrophoresis and immunoblot analysis of Chinese hamster ovary (CHO) cell lysates, we have shown for the first time that high molecular weight complexes containing gp96 form in vivo. It is not immediately clear whether the observed complexes are gp96 homooligomers or protein complexes containing both gp96 and other proteins. We are developing concanavalin A batch chromatography and immunoprecipitation protocols to purify the complexes so that their protein content can be determined by a combination of one- and two-dimensional electrophoresis and immunoblotting. |
|
Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, March 26, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Division of Chemical Education |