With the steady developments in the field of laboratory experiments done around the world and shift from radio-immuno-assay to ELISA, present some practical implications about ELISA.
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The conjugate used must be a highly reactive antibody coupled to an enzyme with a high turnover number.
Alkaline phosphatase and horse-raddish-peroxidase are commonly used enzymes.
Glyceraldehydes is a popular coupling agent but requires reactive amino groups to be a part of the enzyme as well as the ...
How will each of the following changes in condition alter the rate of an enzyme-catalyzed reaction:
-decreasing temp to 10 deg C?
-increasing the pH of the solution from 7 to 11?
-heating only the enzyme to 100 deg C?
You characterize a new enzyme's kinetics. Using a saturating (very high so all E is ES) substrate concentration, you measure the initial rate of the reaction at various enzyme concentrations. Does this data fit the Michaelis Menton model/equation? If not, what may be happening?
E (nM), rate (mM,s)
5, 50
10, 225
15
In the presence of the enzyme alcohol dehydrogenase, the rate of reduction of acetaldehyde to ethanol increases as you increase the concentration of the substrate, acetaldehyde. Eventually the rate of the reaction reaches a maximum, where further increases in the concentration of the substrate has no affect on the reaction rate.
The KM of a Michaelis-Menten enzyme for a substrate is 1.0 x 10-4 M. At a substrate concentration of 0.2 M, Vo=43x10^-6 M for a certain enzyme concentration. However, with a substrate concentration of 0.02 M, Vo has the same value.
(A) Using numerical calculations show that this observation is accurate.
(B) What is the best
Compare competitive and noncompetitive in terms of A) how Km is effected in presence of inhibitor, B) how Vmax is effected in presence of inhibitor, C) where inhibitor would bind to the enzyme
Here are the following numbers I have calculated;
We were given a substrate to plot againist velocity and 3 enzymes to plot as well. From the data:
Enzyme A Ki= 2.575 | Kcat = 50 | Km= 3.33
Enzyme B Ki = 10.33 | Kcat = 16.65 | Km = 33.3
Enzyme C Ki= 1.00 | Kcat = 10 | Km = .2
I'm having tr
An enzyme is a large protein molecule (typically with a molar mass greater than 20,000 AMU) that has a structure capable of catalyzing specific biological reactions. In general one or more reactant molecules (called substrates) bind to an enzyme at its "active sites" where the reaction the enzyme is responsible for occurs. The g
