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.
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Answer:
For number 5 it is the 2nd one some stants has a mass of 1.25 g And the 2nd 1 number 6It is the 1st 1A subject has a melting point of 40
Polyatomic ions: 
, 
, 
, 
, 
, and 
Monatomic ions: 
, 
, and 
<h3>Monoatomic vs Polyatomic Ions</h3>
In chemistry, monoatomic ions are ions that consist of only a single type of atom. They are usually positive or negatively charged and are otherwise known as simple ions. Examples include , , and
Polyatomic ions, on the other hand, are ions that consist of more than one atom, unlike monoatomic ions. The two or more atoms are covalently bonded and the entire structure behaves like a single chemical entity in reactions. Polyatomic ions are otherwise known as molecular ions.
Examples of polyatomic ions are , , , , , and
Thus, from the diagram:
- Polyatomic ions: , , , , , and
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Answer:
increase
Explanation:
because in endothermic reaction heat is absorbed
