Hi all,
I have encountered many papers that almost exclusively use insulin, alcohol dehydrogenase and beta-lactalbumin as aggregated client proteins in chaperone assays. Is there a reason why these three proteins are used as the client proteins almost exclusively?
Thanks in advance!
Cece
Hi there,
Insulin is very convenient because it is naturally proned to aggregation after reduction by DTT so using a light scattering assay you have easy access to protective effect of chaperone. For BL, it is about heat induced aggregation (Citrate Synthase might also be used for temperature induced aggregation assay). About ADH, activity is easy to characterize by following NADH formation at 340nm. In this case the protective effect of chaperone may be performed at the protein activity level.
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