A 45-year-old man with chronic alcoholism is found to eliminate blood ethanol at a constant rate of about 7 g per hour whether his blood level is 50 mg/dL or 300 mg/dL. This behaviour is best explained by:
- A Alcohol dehydrogenase operating at less than half-maximal velocity
- B Saturation of alcohol dehydrogenase so that velocity approximates Vmax and is independent of substrate concentration ✓
- C First-order kinetics because ethanol is cleared exponentially
- D Induction of microsomal ethanol oxidising system at all concentrations
Explanation
When substrate concentration greatly exceeds Km, the enzyme is saturated and the reaction follows zero-order kinetics: velocity equals Vmax and does not change with further rises in substrate concentration. Ethanol concentrations achieved after drinking are far above the Km of hepatic alcohol dehydrogenase, giving a fixed elimination rate. Option C describes first-order kinetics, seen only when substrate concentration is well below Km, which does not apply here.
Reference: Lippincott Illustrated Reviews: Biochemistry, 8th ed.
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