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Finding Michaelismenten constant and Vmax 
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#1
Feb1606, 01:12 AM

P: 74

Ok, here is the problem
A singlesubstrate enzyme catalyzed reaction was investigated in the presence of 1.0 mM inhibitor as well as in the absence of inhibitor, the intial substrate concentration being constant throughout. The following results were obtained: intial velocity (uM/min) that is micro Molar per min [S](mM)[I]=0[I] = 1.0mM 5.0161111 6.67194141 10.00263183 20.00400279 50.00576399 Determine the type of inhibition exhibited by I and caluclate the values of Km apparent and Vmax apparent in the presence of 3.0mM inhibitor. Ok i made a Linewaverburk plot, and it looks seems that the inhibitor is a noncompetative inhibitor because it does not change Km but it does change Vmax, but the part i am having trouble with is how to calculate Km apparent and how to calculate Vmax apparent. Will that just be the Km apparent be just the xintercept of the Lineweaverburk plot, and Vmax apparent be the yintercept of the second line where 1.0mM inhibitor was used. I am not sure though because it wants these values at 3.0mM. So can some one help me out please. Thanks 


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