In enzyme inhibition studies, if the uninhibited rate is v0 and the inhibited rate is vi, how is the degree of inhibition defined?
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A(v0 - vi) / v0
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B(v0 + vi) / v0
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C(v0 * vi) / v0
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D(v0 - vi) / vi
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Evi / v0
Answer
Correct Answer: (v0 - vi) / v0
Explanation
Introduction / Context:Quantifying inhibitor impact helps compare compounds and conditions. A simple normalized metric—degree of inhibition—expresses fractional activity loss relative to the uninhibited control.
Given Data / Assumptions:
- Two measured rates: v0 (no inhibitor) and vi (with inhibitor).
- Same assay conditions except for inhibitor presence.
Concept / Approach:Fractional loss relative to the control is computed by subtracting the inhibited rate from the control rate and normalizing by the control: (v0 - vi)/v0. This yields values from 0 (no inhibition) to 1 (complete inhibition).
Step-by-Step Solution:
Compute numerator: difference in rates due to inhibitor, v0 - vi.Normalize by v0 to remove absolute-rate dependence.Degree of inhibition = (v0 - vi)/v0.Verification / Alternative check:Define residual activity as vi/v0; then degree of inhibition = 1 - residual activity = 1 - (vi/v0), which simplifies to (v0 - vi)/v0.
Why Other Options Are Wrong:
- (v0 + vi)/v0 inflates the value; not a loss metric.
- (v0 * vi)/v0 reduces to vi; not normalized to loss.
- (v0 - vi)/vi diverges as vi → 0 and is not bounded by 1.
- vi/v0 is residual activity, not degree of inhibition.
Common Pitfalls:Mixing up residual activity with inhibition, or failing to normalize to the correct baseline.
Final Answer:(v0 - vi) / v0.