Register to reply

Finding Michaelis-menten constant and Vmax

by babbagee
Tags: constant, michaelismenten, vmax
Share this thread:
Feb16-06, 01:12 AM
P: 74
Ok, here is the problem

A single-substrate 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

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 Linewaver-burk 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 x-intercept of the Lineweaver-burk plot, and Vmax apparent be the y-intercept 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.

Phys.Org News Partner Science news on
Study links polar vortex chills to melting sea ice
Lab unveil new nano-sized synthetic scaffolding technique
Cool calculations for cold atoms: New theory of universal three-body encounters

Register to reply

Related Discussions
Finding Gravity Constant Introductory Physics Homework 1
Finding Hydrolysis Constant Biology, Chemistry & Other Homework 1
Finding the dampening constant Introductory Physics Homework 1
Finding a constant General Math 7
Finding Spring Constant Introductory Physics Homework 3