The purpose of the progress curve is to determine if an enzymatic reaction rate remains constant for given concentrations of enzyme and substrate, for a given assay time (20 min). How long did the rate of reaction of WGAP remain constant in your experiments? How do you know? What would cause the reaction rate to not be constant and plateau after some time?

Two-dimensional gel electrophoresis of proteins in a cell extract provides a qualitative way to compare proteins with respect to intra- cellular abundance. Describe a quantitative approach to the deter- mination of number of molecules of an enzyme per cell.

If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?

You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place.  Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place.  Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.