WHAT IS LIFE? ACHIEVE 1 TERM ACCESS CODE
5th Edition
ISBN: 9781319516116
Author: PHELAN
Publisher: MAC HIGHER
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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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Check out a sample textbook solutionStudents have asked these similar questions
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
The part of hemoglobin that binds iron is
O alpha globulin 2
Obeta globulin 2
alpha globulin 1
O beta globulin 1
heme
According to Figure 17.10b, at a pH of 7.4, how much hemoglobin is unloaded in the tissue?
12%
24%
56%
72%
95%
Chapter 22 Solutions
WHAT IS LIFE? ACHIEVE 1 TERM ACCESS CODE
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- What statement about hemoglobin's integrated transport of oxygen, carbon dioxide and protons is FALSE? Question 26 options: Lower pH leads to more oxygen being released into the tissues Protons can bind hemoglobin at a variety of sites, including histidine side chains. Proton binding stabilizes the R-form of hemoglobin. Hemoglobin binds bicarbonate and transports it from the tissues to the lungs Carbon dioxide binds to hemoglobin in the tissues and gets transported back to the lungsarrow_forwardI 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
- I’m not sure how this will increase or decrease oxygen concentration can you please help?arrow_forwardI believe I use the diffusion law on this: (Diffusion Constant × ∆Concentration × Area) / Thickness. Then change the constant into micrometers (x10^-12). Maybe use the fact that oxygen = 16 grams/mol. Am I on the right track? Thank you for any help you can provide.arrow_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
- Hemoglobin can exist in one of two forms. What are they?arrow_forwardHemoglobin will bind oxygen and release CO2 in places where there is a higher concentration of O2, lower concentration of CO2, lower temperature and lower acidity (as it is in lungs) and will do the reverse – release oxygen and bind CO2 - in places where there is a lower concentration of O2, higher concentration of CO2, higher temperature and higher acidity (as it is in working muscles). True False While white blood cells never leave the circulation, red blood cells regularly leave it and travel by lymphatic system or find home in other tissues, e.g., lymph nodes, spleen, etc. True False Blood clotting (coagulation) is a complex process involving many factors and it exhibits positive feedback loops: many of the factors also stimulate production of their own precursors. B lymphocytes mature in the thymus while T lymphocytes mature in the bone marrow True False Antibodies are molecules on the surfaces of foreign…arrow_forwardWhich five statements about hemoglobin and myoglobin structure are true? Each iron atom can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Molecular oxygen binds reversibly to Fe²+ in heme. Heme is composed of an organic protoporphyrin component and a metal atom. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron atom. Each hemoglobin or myoglobin molecule can bind four oxygen molecules. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron atom.arrow_forward
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