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Home Biochemical Engineering Enzymes and Kinetics Comments

  • Question
  • The ratio of the amount of a protein present in a sample, which is used as a measure of purification, is known as


  • Options
  • A. specific activity
  • B. relative activity
  • C. purity ratio
  • D. all of these

  • Correct Answer
  • specific activity 


  • Enzymes and Kinetics problems


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    • 1. Which of the following step is assumed to be the slowest step in the Michaelis Menten equation?

    • Options
    • A. The substrate consuming step
    • B. The product releasing step
    • C. Formation of enzyme substrate complex
    • D. None of these
    • Discuss
    • 2. If a reaction occurs in the absence of inhibitor with rate ?0 and in the presence of inhibitor with rate ?i, the degree of inhibition is defined as

    • Options
    • A. (?0 - ?i)/?0
    • B. (?0 + ?i)/?0
    • C. (?0?i)/?0
    • D. (?0-?i)/?i
    • Discuss
    • 3. When an enzyme is functioning at Vmax, the rate of the reaction is limited by

    • Options
    • A. the number of collisions between enzyme and substrate
    • B. the number of substrate molecules in the reaction
    • C. the concentration of the substrate
    • D. the rate at which the enzyme can convert substrate to product
    • Discuss
    • 4. The usual method(s) to solve rate equation of simple enzyme kinetics is/are

    • Options
    • A. Michaelis Menten approach
    • B. Briggs-Haldane approach
    • C. Numerical solution approach
    • D. all of these
    • Discuss
    • 5. For an enzyme that displays Michaelis-Menten kinetics, the reaction velocity (as a fraction of Vmax) observed at [S] = 2 KM will be

    • Options
    • A. 0.09
    • B. 0.33
    • C. 0.66
    • D. 0.91
    • Discuss
    • 6. Which category of enzymes belongs to class 5 in the international classification?

    • Options
    • A. Hydrolases
    • B. Isomerases
    • C. Oxido-reductases
    • D. Cyclase
    • Discuss
    • 7. Predominantly uncompetitive inhibition may be called when

    • Options
    • A. competitive inhibition is greater than uncompetitive inhibition
    • B. competitive inhibition is smaller than uncompetitive inhibition
    • C. competitive inhibition is equal to uncompetitive inhibition
    • D. none of the above
    • Discuss
    • 8. When substrate [S] = KM (Michaelis-Menten constant), the velocity of an enzyme catalyzed reaction is about

    • Options
    • A. 0.1 * Vmax
    • B. 0.2 * Vmax
    • C. 0.5 * Vmax
    • D. 0.9 * Vmax
    • Discuss
    • 9. A classical noncompetitive inhibitor has

    • Options
    • A. no effect on substrate binding
    • B. no effect on substrate binding and vice versa
    • C. significant effect on substrate binding
    • D. significant effect on substrate binding and vice versa
    • Discuss
    • 10. The rate equation in non-competitive inhibition based on Michaelis Menten equation is given by

    • Options
    • A. rmaxS/(Km + S)(1+I/Ki)
    • B. rmaxE/(Km (1+I/Ki)+S))
    • C. VmaxS/(Km + S)(1+I/Ki)
    • D. rmaxS/Km
    • Discuss


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