Loose-leaf Version for What Is Life? A Guide to Biology 4E & LaunchPad for What is Life? A Guide to Biology 4E (Twelve Month Access)
4th Edition
ISBN: 9781319154639
Author: Jay Phelan
Publisher: W.H. Freeman & Co
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Question
Chapter 22, Problem 12SA
Summary Introduction
To analyze:
Whether the hemoglobin in individuals living at higher altitudes would be more ‘sticky’ or less ‘sticky’.
Introduction:
The availability of oxygen at higher altitudes is lower. So, adaptations are necessary to take up oxygen, efficiently.
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Students have asked these similar questions
Suppose Gina climbs a high mountain where the oxygen partial pressure in the air decreases to 70 torr. Assume that the pH of
her tissues and lungs is 7.4 and the oxygen concentration in her tissues is 20 torr. The P50 of hemoglobin is 26 torr. The degree
of cooperativity of hemoglobin, n, is 2.8.
Estimate the percentage of the oxygen-carrying capacity that she utilizes. Calculate your answer to one decimal place.
сараcity:
%
In 1913, Archibald Hill described an alternative formulation for cooperative processes such as the binding of oxygen by
hemoglobin by considering the hypothetical equilibrium
Hb+ n0₂ Hb(0₂)n
2
Analysis leads to the Hill equation:
n
p02₂"
(
Y
log (₁ x x ) = log
Y
(^_^)
log
where Y is the fractional saturation. This equation suggests that a plot of log
with slope n.
Plots for myoglobin and hemoglobin are shown here:
3
2
1
O
-1
-2
-3
P50
+
n
= nlog (pO,) – n log(P5o)
Myoglobin
(0.25, -0.25)
-1 0 1
2
log (pO₂)
(3.0, 2.5)
3 4
(^_^)
log
3
2
1
O
-1
-2
-3
-4
(0, -3.4)
-1
0
Y
Y
versus log (pO₂) should yield a line
Hemoglobin
(2.1, 2.5) -
(0.7, -2.0)
(1.9, 1.3)
(0.4, -3.5)
1
2
log (pO₂)
- (2.4, 2.4)
3 4
In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.
Chapter 22 Solutions
Loose-leaf Version for What Is Life? A Guide to Biology 4E & LaunchPad for What is Life? A Guide to Biology 4E (Twelve Month Access)
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- I am eating a snack as I type this question. My body is breaking down the food to provide energy so that my muscles will continue to contract and I can continue to type. During this process, some acidic byproduct could be produced, decreasing the the pH in my muscles. a) What effect will this have on the structure of hemoglobin. (Briefly describe. No more than 2-3 sentences.) b) What effect does this have on the Pso of hemoglobin?arrow_forwardTo demonstrate an understanding of oxyhemoglobin binding, insert a word from the list in each blank to complete the statements. Not all terms will be used. increased A right shift of the oxy-hemoglobin curve signifies a affinity for oxygen. hold acidic A temperature will cause a right shift of the oxy- hemoglobin curve. basic A more pH than normal blood pH will cause a right shift higher of the oxy-hemoglobin curve. As a person exercises, their muscles give off heat which raises the temperature of the blood. This will cause hemoglobin to more oxygen at the cells. lower release decreasedarrow_forward(b) The diagram on the right illustrates the change in the p50 (partial pressure of O2 required to achieve 50% saturation) of hemoglobin and the 2,3-bis-phosphoglycerate (BPG) concentration in the erythrocytes of a person who spent 6 days hik- ing in the Andes Mountains of Peru. As the hiker climbs to higher and higher altitudes, the atmos- pheric pressure, including the partial pressure of O2, decreases. Yet the p50 increases, making it less favorable to achieve saturation of the hemo- globin. Explain. Pso (torr) Sea level 34 33- 32 31 30- 29 28 27 26 4530 m above- sea level (c) If individuals with the following mutant hemo- globins accompanied the hiker, evaluate the degree of respiratory distress that they would experience despite the increased erythrocyte BPG concentration. (In the ta- ble of mutants on the right, the mutation His(143)Asp, for instance, means that the His residue that occurs at se- quence position 143 on the ß-chain has been substituted by Asp.) Describe the…arrow_forward
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