Answer:
0.7μM = 0.6 μM = 0.5 μM > 0.4 μM > 0.3 μM > 0.2 μM
Explanation:
An enzyme solution is saturated when all the active sites of the enzyme molecule are full. When an enzyme solution is saturated, the reaction is occurring at the maximum rate.
From the given information, an enzyme concentration of 1.0 μM Y can convert a maximum of 0.5 μM AB to the products A and B per second means that a 1.0 M Y solution is saturated when an AB concentration of 0.5 M or greater is present.
The addition of more substrate to a solution that contains the enzyme required for its catalysis will generally increase the rate of the reaction. However, if the enzyme is saturated with substrate, the addition of more substrate will have no effect on the rate of reaction.
<em>Therefore the reaction rates at substrate concentrations of 0.7μM, 0.6 μM, and 0.5 μM are equal. But the reaction rate at substrate concentrations of 0.2 μM is lower than at 0.3 μM, 0.3 μM is lower than 0.4 μM and 0.4 μM is lower than 0.5 μM, 0.6 μM and 0.7 μM.</em>
Answer:
I got the answers but it won't let me post it correctly on here....
Explanation:
9.) 10-2.76 =0.0174 [H30+]= 1.74*10-3 M
10.)10-3.65=0.00224 [H3O+] =2.24*10-2 M
11.)10-3.65=0.00224 [OH-]= 2.224*10-4M
12.)10-6.87=0.00000135 [OH-]= 1.35*10-7M
Answer:
2.24 Liters are in 4.4 grams of CO2 at STP
The name isovolumetric indicates that there is no change in volume that takes place and this only occurs when all of the valves within the heart are shut.
Given:
0.607 mol of the weak acid
0.609 naa
2.00 liters of solution
The solution for finding the ph of a buffer:
[HA] = 0.607 / 2.00 = 0.3035 M
[A-]= 0.609/ 2.00 = 0.3045 M
pKa = 6.25
pH = 6.25 + log 0.3045/ 0.3035 = 6.25 is the ph buffer prepared.
