Hello
For typical dose-response assays, our lab usually uses steady state intervals for defining the difference between control and tested compound. For those assays, we typically use the angular coefficient or end-point value of given curve (within steady state) to estimate percentage of inhibition, or even kinetic constants
Now we have being working with an enzyme with strong 'sigmoidal' time curse reaction (hill n=3). How can I mathematically compare curves between control and inhibited reactions, or calculate constants?
If anyone could please point me to a good theorical reference or literature examples, I will be very thankful
Stay all safe
The simplest way is to pick a specific time point as the point at which to calculate % inhibition. This is purely phenomenological. No theory.
If you have an enzyme reaction that shows a time lag before reaching maximal rate, you should investigate the reason for it. Maybe the enzyme autoactivates in the presence of its substrate, like an autophosphorylating kinase, or the substrate may slowly displace a competitive inhibitor. You may be able to preactivate the enzyme so as to get Michaelis-Menten behavior.
Time lags can also occur in coupled enzyme reactions if the concentration of the 2nd enzyme in the sequence is not high enough.
Hello :
You can calculated the inititial velocity (enzyme activity) from the linear section of the curve when the slope was in its maximal value.
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