Biology
5th Edition
ISBN: 9781260487947
Author: BROOKER
Publisher: MCG
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Chapter 48.9, Problem 1CC
Summary Introduction
To determine: The possible effects that are produced to the position of the middle curve, when bicarbonate ions (HCO3-) are added into the blood of resting, healthy individual.
Introduction: The process of circulation inside the body of an organism is responsible for the transportation of oxygen and various nutrients. The purpose of circulation is to fulfil the demands of the tissues and organs and maintains the internal environment of the body. The blood is the responsible carrier that transports various types of
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Figure 6 shows the binding of oxygen to myoglobin and haemoglobin (Y-axis: Fraction
saturation) when they are exposed to various partial pressures of oxygen (X-axis: pO2).
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Myoglobin
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Hemoglobin
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Po, (kPa)
Figure 6
(i)
Briefly compare the protein structure of myoglobin to that of haemoglobin.
(ii)
Based on Figure 6, explain the differences between the functions performed by
myoglobin and haemoglobin.
Fraction saturation
In the text, we learned that BPG is abundantly present in erythrocytes to greatly reduce the affinity of hemoglobin for oxygen. When 2,3-BPG binds to deoxyhemoglobin, it acts to stabilize the low oxygen affinity state (T state) of the oxygen carrier. What would happen to hemoglobin if the BPG were removed? Would our body still be able to efficiently deliver oxygen to the tissues?
After spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the concentration of 2,3- bisphosphoglycerate (2,3-BPG) in red blood cells increases. What effect would an increased concentration of 2,3-BPG have on the oxygen-binding curve for hemoglobin? Why would this adaptation be beneficial for functioning well at high altitude?
Chapter 48 Solutions
Biology
Ch. 48.1 - Prob. 1CCCh. 48.1 - Prob. 1CSCh. 48.2 - Core Skill: Connections Leukocytes are part of the...Ch. 48.3 - Prob. 1CCCh. 48.3 - Prob. 2CCCh. 48.4 - Do erythrocytes enter and exit through pores in...Ch. 48.7 - Prob. 1CSCh. 48.7 - Prob. 1CCCh. 48.7 - Prob. 2CCCh. 48.8 - Prob. 1EQ
Ch. 48.8 - Prob. 2EQCh. 48.8 - Prob. 3EQCh. 48.9 - Prob. 1CCCh. 48.10 - Prob. 1CSCh. 48 - Prob. 1TYCh. 48 - Prob. 2TYCh. 48 - A major advantage of a double circulation is that...Ch. 48 - Prob. 4TYCh. 48 - For blood flow through a closed circulation, which...Ch. 48 - Prob. 6TYCh. 48 - The countercurrent exchange mechanism in fish...Ch. 48 - The tracheal system of insects a. consists of...Ch. 48 - Prob. 9TYCh. 48 - Prob. 10TYCh. 48 - Prob. 1CQCh. 48 - Prob. 2CQCh. 48 - Prob. 3CQCh. 48 - Prob. 1COQCh. 48 - List the components of the mammalian respiratory...
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- How does hemoglobin help maintain the oxygen partial pressure gradient during gas transport in the body?arrow_forwardIn 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.arrow_forwardO E-If answers (1), (2), (3) and (4) are TRUE Which of the following is NOT true about the liver lobule? * (1) Bile canaliculi transport bile towards the bile ducts located at the corners of the liver lobule. (2) Sinusoidal capillaries drain into the central vein. (3) Liver lobules are capable of producing plasma proteins such as albumin. (4) The portal arteriole takes blood to the liver lobule, while the portal venule takes blood away from the liver lobule. O A - If answers (1), (2) and (3) are TRUE B - If answers (1) and (3) are TRUE O C- If answers (2) and (4) are TRUE O D- If only answer (4) is TRUE O E- If answers (1), (2), (3) and (4) are TRUE Which of the following is NOT true with regards the oxygen-hemoglobin dissociation curve? * 27°C ere to searcharrow_forward
- Below is the equation that represents O2 binding to hemoglobin. Hb+4O2⇌Hb(O2)According to Le Chatelier’s principle, which form of the hemoglobin (Hb or Hb(O2)4) is predominant in the lungs where the partial pressure of oxygen is high? Explain. I need help answering thisarrow_forwardSuppose you visit the Dalai Lama in Dharamsala, India (elevation 1460 m),and you begin to ponder the “big questions,” such as “What is the fractionalsaturation of the Dalai Lama’s hemoglobin?”(a) Assuming the Dalai Lama’s hemoglobin has a Hill coefficient = 3.2,and a P50 = 31 mm Hg, calculate the change in fractional O2 saturationof his hemoglobin going from his lungs (where PO2 = 85 mm Hg) to hiscapillaries (where PO2 = 25 mm Hg).(b) Why do you suppose the Dalai Lama’s hemoglobin has a P50 higher thannormal (where “normal” = 27 mm Hg)?arrow_forwardCalculate the average ml of oxygen molecules in 100 ml blood in the athletes at low altitude and then in athletes in high altitude while training at high altitude. Use the following information: 1.39 ml of oxygen per gram of hemoglobin. Do athletes training at high altitudes have more or less oxygen molecules per ml of blood then athletes training at low altitudes? Explain why this difference gives athletes who train at high altitudes an advantage over athletes who train only at low altitudes.arrow_forward
- (b) The diagram on the right compares O2-dissoci- ation curves for human hemoglobins characterized by dif- ferent p50 values. If Ko2 represents the equilibrium disso- ciation constant for oxygen binding, e.g., Hb(02)n Hb + nO₂ show the relationship between Ko2 and p50. Assign one of the curves (a, b, e) that best approxi- mates the Ko2 of each of the mutant hemoglobins in the table above including HbA where Ko2 represents the equi- librium dissociation constant for oxygen binding. If no curve is present for any of the mutant hemogobins, state the rea- son why the mutant is not represented. Indicate on the graph where its p50 would lie. PERCENT SATURATION 100- 80- 60- 40- 20- PARTIAL PRESSURE OF OXYGEN lungs veins muscle 0- 0 20 bc/d T 100 120 140 40 60 80 OXYGEN PRESSURE (millimeters of mercury) (c) Of the mutant hemoglobins in the table above, which form a hydrogen bond stabilizing the R (oxy) conformation similarly to that in wild type HbA. Justify this statement on the basis of the…arrow_forwardThe dotted lines in the two graphs below represent a shift in the oxygen-hemoglobin dissociation curve. Which shift would allow more oxygen delivery to the tissues? Name three conditions in the tissues that would cause thecurve to shift this way.arrow_forward100 80 60 40 20 40 60 80 100 Po, (mm Hg) Percent oxygen saturation Hemoglobin/myoglobin 20arrow_forward
- Table 4: Presence or Absence of Agglutination Mother 1 Father 1 Child 1 Mother 2 Father 2 Child 2 Mother 3 Father 3 Child 3 Anti-A Sera Agglut No Agglut No No No Agglut No Agglut Anti-B Sera Agglut No No No Agglut Agglut No No No Anti-Rh Sera No Agglut Agglut Agglut No Agglut No No No Blood Type AB- O+ A+ 0+ B- B+ A- O- A-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_forwardWhich of the following is the concentration of hemoglobin-bound oxygen in the blood when the heme is fully saturated? 8500 uM 8630 uM 2200 uM 8800 uMarrow_forward
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