Stability of Monomeric Gamma Crystallins in the Presence of Heat
Gamma crystallins found in the eye form cataracts when they aggregate. In order to investigate the interactions between crystallins that can lead to aggregates, our research focused on the stability of the monomer. Understanding what can degrade, unfold or cause a monomer to act as protomers will help understand how crystallins are able to form non-monomeric species and if non-monomeric species can be reverted to monomer. Gamma crystallin monomers were electrophoresed by polyacrylamide gel in the presence of heat, but in the absence of denaturing chemicals SDS and DTT, no protein was observed. When the protein was not heated, this phenomenon was not observed. We have attempted to change variables in this experiment by running on native gels, reducing voltage, reducing temperature, and attempting to inhibit possible proteases. We are still working on understanding why the monomer seems to disappear in the presence of only heat.
Keywords: Gamma crystallins, SDS-PAGE, Protein aggregation
Topic(s):Biochemistry and Molecular Biology
Presentation Type: Oral Paper
Session: 311-5
Location: MC 212
Time: 2:30