If an inhibitor is uncompetitive, i.e inhibits by binding to ES complex, thus decreasing the Km and Vmax value and if another inhibitor is non- competitive, i.e it inhibits by decreasing the activity of the enzyme without changing the affinity, what is the explanation that when both are added, there is no additive inhibition of the enzyme?
John Tainer
It matters how you did this experiment. Did you try looking at the linear part of the inhibitor curve for each type of inhibitor and then titrating in the other type of inhibitor? I would expect you will see added inhibition is you do the experiment measuring changes in the linear part of the inhibitor cure at 50% inhibition.
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