Homework Answers
![t = km 1 + 1 ud Y Vmax [s] max kms Michaelis menten Constant Vmaxs is the maximum reaction a velocity from the graph =1258 +](http://img.homeworklib.com/questions/15f70680-1fc1-11ec-9079-cd39a7d19d89.png?x-oss-process=image/resize,w_560)
Add Answer to:
The activity of an enzyme was tested in the presence of a mixed type of inhibitor....
The effect of an inhibitor on an enzyme was tested and the experiment gave the results...
The effect of an inhibitor on an enzyme was tested and the experiment gave the results below. Plot on Excel the data using a double-reciprocal plot (Lineweaver-Burke), determine Km and Vmax of the no inhibitor and each type of inhibitor and the type of inhibition that is occurring. [S] µM V (µmol/min) V (µmol/min) V (µmol/min) with 0.0 nM with 25 nM with 50 nM Inhibitor Inhibitor Inhibitor ______ ___________ ___________ ___________ 0.4 0.22 0.21 0.20...
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor....
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
The following data was obtained for an enzyme in the absence of an inhibitor, and in...
The following data was obtained for an enzyme in the absence of an inhibitor, and in the presence of two different inhibitors. The concentration of each inhibitor was 10 mM. The total concentration of enzyme was the same for each experiment. [S] {mM} without inhibitor v, {umol/(ml*s)} with inhibitor A v, {umol/(ml*s)} With inhibitor B v, {umol/(ml*s)} 0.0 0.0 0.0 0.0 1.0 3.6 3.2 2.6 2.0 6.3 5.3 4.5 4.0 10.0 7.8 7.1 8.0 14.3 10.1 10.2 12.0 16.7 11.3...
For a report, after plotting the lineweaver-burk plot for a protease enzyme with and without inhibitor....
For a report, after plotting the lineweaver-burk plot for a protease enzyme with and without inhibitor. It shows that the km value increases in the presence of inhibitor and Vmax decreases. what type of inhibition is it? The inhibitor is an azide.
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor....
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed non-competitive kinetics with y- intercepts of 15s -1 and 5 s -1 in the presence and absence of the inhibitor respectively. If the inhibitor binding constant was 0.5nM, calculate [I ] used in this reaction? a. 0.135nM b. none of the above c. 0.225nM d. InM e. 0.125nM
Please show me how to solve these and I'll give thumbs up. Thank you! Question 6...
Please show me how to solve these and I'll give thumbs up.
Thank you!
Question 6 O out of 10 points An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with X- intercepts of -10mM -1 and -3.5mM-1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? Question 7 O...
An enzyme-catalyzed reaction to the presence of 5 nM of reversible inhibitor yields a Vmax value...
An enzyme-catalyzed reaction to the presence of 5 nM of reversible inhibitor yields a Vmax value that is 80% of the value in absence of the inhibitor. The KMvalue is unchanged. a) what type of inhibition is occurring? b) what proportion of the enzyme molecule will have bound inhibitor? c) Draw the Lineweaver-Burk (known as double-reciprocal plot) for uninhibited and inhibited reaction. SHOW ALL YOUR WORK PLEASE
please explain and answere Question 11 (1 point) A competitive inhibitor has [1] = 269 uM....
please explain and answere
Question 11 (1 point) A competitive inhibitor has [1] = 269 uM. The y-intercept for the Lineweaver-Burke plot is 9900 s*um 1. The x-intercept for the Lineweaver-Burke plot in the presence of the inhibitor is -0.0040 MM 1. Km for the uninhibited is 32 uM. Calculate the Ki for the inhibitor in uM. Round your answer to the nearest whole number (i.e. if you calculated 10.03, input your answer as 10) Your Answer: Your Answer
A class conducts an enzyme kinetics experiment using the digestive enzyme, trypsin and an unknown inhibior....
A class conducts an enzyme kinetics experiment using the
digestive enzyme, trypsin and an unknown inhibior. They generate
the two curves below. According this data, what type of inhibitor
did the students use?
1. Competitive 2. Non- Competitive
In the same Lineweaver-Burke plot from question above, what is
the approximate value of Vmax?
1/4
100
0.01
Vmax cannot be determined from this plot.
An experiment was performed to determine the effects of an inhibitor on the breakdown of glycogen...
An experiment was performed to determine the effects of an inhibitor on the breakdown of glycogen by an enzyme. In an accompanying experiment, the inhibitor was added to the glycogen-enzyme suspension and reacted using the same experimental conditions. The data obtained from these experiments is tabulated below. Draw the Michaelis-Menten and Lineweaver-Burke plots of these data. Determine the form of inhibition observed from these results and explain your rationale for this form. Determine the values for K_m and V_max from...
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed non-competitive kinetics with y- intercepts of 15s -1 and 5 s -1 in the presence and absence of the inhibitor respectively. If the inhibitor binding constant was 0.5nM, calculate [I ] used in this reaction? a. 0.135nM b. none of the above c. 0.225nM d. InM e. 0.125nM
Please show me how to solve these and I'll give thumbs up.
Thank you!
Question 6 O out of 10 points An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with X- intercepts of -10mM -1 and -3.5mM-1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? Question 7 O...
please explain and answere
Question 11 (1 point) A competitive inhibitor has [1] = 269 uM. The y-intercept for the Lineweaver-Burke plot is 9900 s*um 1. The x-intercept for the Lineweaver-Burke plot in the presence of the inhibitor is -0.0040 MM 1. Km for the uninhibited is 32 uM. Calculate the Ki for the inhibitor in uM. Round your answer to the nearest whole number (i.e. if you calculated 10.03, input your answer as 10) Your Answer: Your Answer
A class conducts an enzyme kinetics experiment using the
digestive enzyme, trypsin and an unknown inhibior. They generate
the two curves below. According this data, what type of inhibitor
did the students use?
1. Competitive 2. Non- Competitive
In the same Lineweaver-Burke plot from question above, what is
the approximate value of Vmax?
1/4
100
0.01
Vmax cannot be determined from this plot.
An experiment was performed to determine the effects of an inhibitor on the breakdown of glycogen by an enzyme. In an accompanying experiment, the inhibitor was added to the glycogen-enzyme suspension and reacted using the same experimental conditions. The data obtained from these experiments is tabulated below. Draw the Michaelis-Menten and Lineweaver-Burke plots of these data. Determine the form of inhibition observed from these results and explain your rationale for this form. Determine the values for K_m and V_max from...
Most questions answered within 3 hours.
-
Where is the error in this code sequence?
String s1 = "Hello";
String s2 = "ello";...
asked 11 months ago -
Financial data for Joel de Paris, Inc., for last year
follow:
Joel de Paris, Inc.
Balance...
asked 11 months ago -
Consider this reaction:
Al2(SO4)3 (aq)+ BaCl3
(aq) Al2Cl6 (aq)- +
3BaSO4(s) . What is the...
asked 11 months ago -
Suppose that Savneet is considering increasing her
recent random sample from 20 car rentals to 40...
asked 11 months ago -
Trucks arrive at an unloading terminal at an average rate of 120
per hour.
Trucks arrive...
asked 11 months ago -
Why are methanol and ethanol completely soluble in water while
octanol is not very little soluble....
asked 11 months ago -
A facilities manager at a university reads in a research report
that the mean amount of...
asked 11 months ago -
When the CuSO4 is rehydrated by adding water to the anhydrous
compound, is this an endothermic...
asked 11 months ago -
A ray of sunlight is passing from diamond into crown glass; the
angle of incidence is...
asked 11 months ago -
A block of mass 0.249 kg is placed on top of a light, vertical
spring of...
asked 11 months ago -
how do the kidneys compensate in the presences of acidosis
a) trigger hyperventilate
b) reserve acid...
asked 11 months ago -
Question 501 pts
The rental rate of capital to the firm increases. Which of the
following...
asked 11 months ago