Using the Michaelis-Menten equation competitive inhibition, the Inhibition constant, Ki of the inhibitor is 53.4 μM.
<h3>What is the Ki for the inhibitor?</h3>
The Ki of an inhibitor is known as the inhibition constant.
The inhibition is a competitive inhibition as the Vmax is unchanged but Km changes.
Using the Michaelis-Menten equation for inhibition:
Making Ki subject of the formula:
where:
- Kma is the apparent Km due to inhibitor
- Km is the Km of the enzyme-catalyzed reaction
- [I] is the concentration of the inhibitor
Solving for Ki:
where
[I] = 26.7 μM
Km = 1.0
Kma = (150% × 1 ) + 1 = 2.5
Ki = 26.7 μM/{(2.5/1) - 1)
Ki = 53.4 μM
Therefore, the Inhibition constant, Ki of the inhibitor is 53.4 μM.
Learn more about enzyme inhibition at: brainly.com/question/13618533
Answer:
Molarity.
Explanation:
- The molarity (M) of a solution is defined as the no. of moles of solute that dissolved in 1.0 liter of the solution.
M = (mass / molar mass) of the solute (1000 / volume of the solution).
<em>So, the best measurement of concentration for describing the concentration of a solid solute dissolved in one liter of a liquid solution is Molarity.</em>
Answer:
31.36 Liters
Explanation:
1 mole is equal to 22.4 liters at STP so you can use the equation
1.4 moles * 22.4 liters
to find the volume.
Answer:
It contain double Bond.
Explanation:
To determine weather the bond is double or triple simply check the electron involved in mutual sharing of an electron if 2 electron takes parts it said to be double or if 3 it said to be triple.
The decrease in velocity is called deceleration or negative acceleration.
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