Answer:
its made up of both but I would probably say kinetic
Explanation:
Answer:
6.34917360^25g
Explanation:
It's been a while since I've done this type of problem so I'm not making any promises that its right hahaha, but I hope it helps anyway. Please let me know whether I'm right or not!
Given what we know, we can confirm that if further increases in substrate concentration do not result in further increases in reaction rate, then an enzyme is likely saturated.
<h3>What does it mean for an enzyme to be saturated?</h3>
Enzymes work by binding to the substrate in specific zones of the enzyme. The zones are known as the active sites on enzymes. Since enzymes have a limited amount of these zones, once they are all bonded to a substrate, we can say that it is saturated.
Therefore, the saturation of enzymes allows us to explain how further increases in substrate concentration do not result in further increases in reaction rate.
To learn more about enzymes visit:
brainly.com/question/24811456?referrer=searchResults
Answer:
There are 0.93 g of glucose in 100 mL of the final solution
Explanation:
In the first solution, the concentration of glucose (in g/L) is:
15.5 g / 0.100 L = 155 g/L
Then a 30.0 mL sample of this solution was taken and diluted to 0.500 L.
- 30.0 mL equals 0.030 L (Because 30.0 mL ÷ 1000 = 0.030 L)
The concentration of the second solution is:

So in 1 L of the second solution there are 9.3 g of glucose, in 100 mL (or 0.1 L) there would be:
1 L --------- 9.3 g
0.1 L--------- Xg
Xg = 9.3 g * 0.1 L / 1 L = 0.93 g
Answer:
take the l my gang tfdfhngtyhggggggfggg