Primer 3 - Pharmacokinetics

Question 1

What is first order velocity?

Answer 1

More substrate leads to faster reaction. Reaction velocity is directly proportional to the concentration of substrate.

Question 2

What is Km and its equation?

Answer 2

Km is Michaelis constant where it finds the amount of substrates needed to get to half of Vmax.
Km = [S] at 1/2Vmax

Question 3

What is zero order kinetics?

Answer 3

Velocity is independent of substrate concentration.

Question 4

What is Vmax?

Answer 4

It is when the reaction reaches zero order kinetics.

Question 5

How do we control Vmax?

Answer 5

Controlling the amount of enzyme. More enzyme leads to higher Vmax, less, to lesser Vmax.

Question 6

What does Km reflect?

Answer 6

Km reflects the affinity of the enzyme for its substrate. If the affinity is strong, it will take less time to reach 1/2Vmax, which equals to lower Km.

Question 7

What are the X and Y in a Lineweaver-Burk plot?

What is the slope in this graph?

Answer 7

X: 1/[S] and Y: 1/[V].

Slope is Km/Vmax.

Question 8

What is the equation to find where the slope meets X and when it meets Y in a Lineweaver-Burk plot?

Answer 8

X: 1/-Km and Y: 1/Vmax.