I'm testing the effects of denaturants on my enzyme, and incubation of the enzyme with 0.5 M Gdn-HCl (4h) gives me a significant increase in enzyme activity (almost double that of control). The fluorescence spectrum looks pretty normal. Does anyone know what kind of structural/conformational changes might occur in this experimental condition? I'm doing CD spectroscopy next week, that could give some ideas. Has someone got similar results/can explain?
Do you have a purified enzyme? It is possible that 0.5N Gdn has a small effect at the conformation, or it causes the dissociation of some molecule bound to the enzyme, or dissociation of a possible oligomer. There are several explanations, and it is not rare that behaviour. Go ahead about CD, but probably the differences would not be significant.
Thanks :) My enzyme is a tetramer, and the dissociation of oligomer could be a possible reason. Is there any way to check this apart from gel filtration?
- Badges
- Science topic
- Similar topics
- Biological Science
- Biochemistry
- Enzymology
- Enzymes