Forgive me, I've always been terrible at kinetics.
So in our last lab we combined a phosphate buffer, L-Dopa, and tyrosinase (5 trials with different amounts of tyrosinase). For each trial, we took the absorbance values (470nm) every 30 seconds.
We then did the same thing with a constant amount of tyrosinase and a cinnamic acid inhibitor, but varying levels of dopa.
Now I'm trying to figure out the tyrosinase levels in the first experiment.
I graphed the 5 trials where it is absorbance vs time (mins).
I've tried the equation c=A/El and got an answer in M/min for each of the 5 trials which I converted to μmoles/min. My book tells me to also calculate μmoles of product formed per minute, but I'm not sure what that means...
I am also told to graph rate (μmoles/min) vs enzyme concentration in each assay (mg) but I'm also not sure what the latter is.
For the second experiment, I can analyze a double reciprocal plot... I just may have trouble getting that plot. It asks for L-Dopa concentration per assay, which might be the only thing I'm stuck on. Is that the substrate concentration?
Any help is appreciated.