It is possible to distinguish between an irreversible inhibitor and a classical mixed type reversible inhibitor by measuring Vmax of the enzymatic reaction as a function of [E]t in the absence and presence of the inhibitor.
What does the slope represent in each case?
What does the X-axis intercept represent in each case?
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As you know, under normal conditions, we may simplify an enzyme catalyzed reaction like this:
E + S ----> ES -----> E + P
Where k1 is the rate constant for the first arrow, k2 is the rate constant for the reverse of the first arrow and k3 is the rate constant for the second arrow.
Under Michaelis-Menton conditions, the rate expression is:
v = (Vmax[S])/(Km + [S])
And Vmax ...
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