Which of the following statements is/are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation... SHOW MORE The CAMP formed by adenyl cyclase does not persist because 5'-Phosphodiesterase activity prevalent in cells hydrolyzes CAMP to give 5'-AMP. Caffeine inhibits 5'-phosphodiesterase activity which promotes the presence of the more active 'a' form of Glycogen Phosphorylase. a If no precautions are taken blood that has been stored for some time becomes depleted in 2-3 BPG which will result in
Which of the following statements is/are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation... SHOW MORE The CAMP formed by adenyl cyclase does not persist because 5'-Phosphodiesterase activity prevalent in cells hydrolyzes CAMP to give 5'-AMP. Caffeine inhibits 5'-phosphodiesterase activity which promotes the presence of the more active 'a' form of Glycogen Phosphorylase. a If no precautions are taken blood that has been stored for some time becomes depleted in 2-3 BPG which will result in
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
Related questions
Question
Which of the following statements is/are TRUE?
![Which of the following statements is/are TRUE?
Multiple answers: Multiple answers are accepted for this question
Select one or more answers and submit. For keyboard navigation... SHOW MORE v
The CAMP formed by adenyl cyclase does not persist because 5'-Phosphodiesterase activity prevalent in cells hydrolyzes
CAMP to give 5'-AMP. Caffeine inhibits 5'-phosphodiesterase activity which promotes the presence of the more active 'a'
form of Glycogen Phosphorylase.
a
If no precautions are taken blood that has been stored for some time becomes depleted in 2-3 BPG which will result in
increased binding of 0, to Hemoglobin with decreased release of 02 to tissues.
Sickle-cell anemia is the consequence of HbS polymerization through hydrophobic contacts between the side chain Vala6
and a pocket in the EF corner of a-subunits.
d
Decreasing the free energy of activation decreases the reaction rate.
e
The catalytic efficiency of an enzyme cannot exceed the diffusion rate of encounters between E and S.
f
When [S] = Km the velocity = Vmax/2.
Lineweaver-Burk double reciprocal (1/V vs. 1/S) plots convert the hyperbolic Michaelis-Menten V vs. S plot into a straight
line.
According to the Michaelis-Menten equation the v/Vmax ratio = 0.4 when [S] = 4 Km.
i
If V,
= 100 umol/mL/sec and Km = 2 mM the velocity of the reaction when [S] = 20 mM is 10 µmol/mL/sec.
max](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F19c0cbf8-360a-48f7-9f18-2844f13d44ab%2F654321cc-c00b-4562-ad13-1946ad8a6c5e%2Fgyml9im_processed.png&w=3840&q=75)
Transcribed Image Text:Which of the following statements is/are TRUE?
Multiple answers: Multiple answers are accepted for this question
Select one or more answers and submit. For keyboard navigation... SHOW MORE v
The CAMP formed by adenyl cyclase does not persist because 5'-Phosphodiesterase activity prevalent in cells hydrolyzes
CAMP to give 5'-AMP. Caffeine inhibits 5'-phosphodiesterase activity which promotes the presence of the more active 'a'
form of Glycogen Phosphorylase.
a
If no precautions are taken blood that has been stored for some time becomes depleted in 2-3 BPG which will result in
increased binding of 0, to Hemoglobin with decreased release of 02 to tissues.
Sickle-cell anemia is the consequence of HbS polymerization through hydrophobic contacts between the side chain Vala6
and a pocket in the EF corner of a-subunits.
d
Decreasing the free energy of activation decreases the reaction rate.
e
The catalytic efficiency of an enzyme cannot exceed the diffusion rate of encounters between E and S.
f
When [S] = Km the velocity = Vmax/2.
Lineweaver-Burk double reciprocal (1/V vs. 1/S) plots convert the hyperbolic Michaelis-Menten V vs. S plot into a straight
line.
According to the Michaelis-Menten equation the v/Vmax ratio = 0.4 when [S] = 4 Km.
i
If V,
= 100 umol/mL/sec and Km = 2 mM the velocity of the reaction when [S] = 20 mM is 10 µmol/mL/sec.
max
Expert Solution

This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution!
Trending now
This is a popular solution!
Step by step
Solved in 2 steps

Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Recommended textbooks for you

Chemistry
Chemistry
ISBN:
9781305957404
Author:
Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:
Cengage Learning

Chemistry
Chemistry
ISBN:
9781259911156
Author:
Raymond Chang Dr., Jason Overby Professor
Publisher:
McGraw-Hill Education

Principles of Instrumental Analysis
Chemistry
ISBN:
9781305577213
Author:
Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:
Cengage Learning

Chemistry
Chemistry
ISBN:
9781305957404
Author:
Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:
Cengage Learning

Chemistry
Chemistry
ISBN:
9781259911156
Author:
Raymond Chang Dr., Jason Overby Professor
Publisher:
McGraw-Hill Education

Principles of Instrumental Analysis
Chemistry
ISBN:
9781305577213
Author:
Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:
Cengage Learning

Organic Chemistry
Chemistry
ISBN:
9780078021558
Author:
Janice Gorzynski Smith Dr.
Publisher:
McGraw-Hill Education

Chemistry: Principles and Reactions
Chemistry
ISBN:
9781305079373
Author:
William L. Masterton, Cecile N. Hurley
Publisher:
Cengage Learning

Elementary Principles of Chemical Processes, Bind…
Chemistry
ISBN:
9781118431221
Author:
Richard M. Felder, Ronald W. Rousseau, Lisa G. Bullard
Publisher:
WILEY