for normal hemoglobin in blood is represented by curve "D," at a pH concentration of 5mM BPG and 26 mM CO2. O₂ saturation (%) 100 80 A B 60 40 20 20 D E normal Hb 40 60 80 Po₂ (mmHg) 100 1. How would changes to acidity, BPG concentration and CO₂ levels a affinity curve and p50? 1. BPG concentration is decreased to 3mM: The binding affinity cur like B. The p50 would be lower than normal (D). 2. pH is increased to 7.6: The binding affinity curve would look like be [Select] normal (D).
for normal hemoglobin in blood is represented by curve "D," at a pH concentration of 5mM BPG and 26 mM CO2. O₂ saturation (%) 100 80 A B 60 40 20 20 D E normal Hb 40 60 80 Po₂ (mmHg) 100 1. How would changes to acidity, BPG concentration and CO₂ levels a affinity curve and p50? 1. BPG concentration is decreased to 3mM: The binding affinity cur like B. The p50 would be lower than normal (D). 2. pH is increased to 7.6: The binding affinity curve would look like be [Select] normal (D).
Human Physiology: From Cells to Systems (MindTap Course List)
9th Edition
ISBN:9781285866932
Author:Lauralee Sherwood
Publisher:Lauralee Sherwood
Chapter11: The Blood
Section: Chapter Questions
Problem 1SQE
Related questions
Question
![Below are multiple oxygen binding affinity curves for hemoglobin. The affinity curve
for normal hemoglobin in blood is represented by curve "D," at a pH of 7.2 and at a
concentration of 5mM BPG and 26 mM CO2.
O₂ saturation (%)
100
Answer 1:
B
Answer 2:
[Select]
Answer 3:
B
Answer 4:
80 A
60
1. How would changes to acidity, BPG concentration and CO₂ levels affect the binding
affinity curve and p50?
lower than
Answer 5:
E
40
1. BPG concentration is decreased to 3mM: The binding affinity curve would look
like B. The p50 would be lower than normal (D).
2. pH is increased to 7.6: The binding affinity curve would look like B. The p50 would
be [Select]
normal (D).
20
3. CO₂ concentration is increased to 30 mM: The binding affinity curve would look
like. [Select]
The p50 would be
Answer 6:
0
normal (D).
II. The hemoglobin has been treated with a denaturing solution which disrupts
quaternary structure only, and has a binding affinity resembling myoglobin. The
binding affinity curve would look like [Select]
The p50 would
be higher than normal (D).
lower than
Answer 7:
A
Answer 8:
higher than
B/
T
20
D
E
higher than
normal Hb
T
40 60
80 100 120
Po, (mmHg)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fa6c5565a-787b-43d3-b23e-780453faf6da%2Fe596ba6f-3ad1-49b1-a4f2-dc4bb6069509%2Fxgkcmxd_processed.png&w=3840&q=75)
Transcribed Image Text:Below are multiple oxygen binding affinity curves for hemoglobin. The affinity curve
for normal hemoglobin in blood is represented by curve "D," at a pH of 7.2 and at a
concentration of 5mM BPG and 26 mM CO2.
O₂ saturation (%)
100
Answer 1:
B
Answer 2:
[Select]
Answer 3:
B
Answer 4:
80 A
60
1. How would changes to acidity, BPG concentration and CO₂ levels affect the binding
affinity curve and p50?
lower than
Answer 5:
E
40
1. BPG concentration is decreased to 3mM: The binding affinity curve would look
like B. The p50 would be lower than normal (D).
2. pH is increased to 7.6: The binding affinity curve would look like B. The p50 would
be [Select]
normal (D).
20
3. CO₂ concentration is increased to 30 mM: The binding affinity curve would look
like. [Select]
The p50 would be
Answer 6:
0
normal (D).
II. The hemoglobin has been treated with a denaturing solution which disrupts
quaternary structure only, and has a binding affinity resembling myoglobin. The
binding affinity curve would look like [Select]
The p50 would
be higher than normal (D).
lower than
Answer 7:
A
Answer 8:
higher than
B/
T
20
D
E
higher than
normal Hb
T
40 60
80 100 120
Po, (mmHg)
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