The figure at right shows hemoglobin P50values for populations of deermice collectedat different altitudes, from sea level (0 m) to~3,000 m. Based on this figure...A. Deermice collected at higher altitudeshave higher blood O2 binding affinityB. Deermice collected at lower altitudes havehigher blood O2 carrying capacityC. Deermice collected at lower altitudes havehigher blood O2 binding affinityD. Deermice collected at higher altitudeshave lower blood O₂ carrying capacityE. None of the above(Torr)P503837363534333231300500Storz 2007 J Mamm88, 24-311000 1500 2000Altitude (m)25003000I3500

Oxygen present in the air diffuses into the blood during respiration via the lungs. Hemoglobin (Hb)…

The figure at right shows hemoglobin P50 values for populations of deermice collected at different altitudes, from sea level (0 m) to ~3,000 m. Based on this figure... A. Deermice collected at higher altitudes have higher blood O₂ binding affinity B. Deermice collected at lower altitudes have higher blood O₂ carrying capacity C. Deermice collected at lower altitudes have higher blood O₂ binding affinity D. Deermice collected at higher altitudes have lower blood O₂ carrying capacity E. None of the above P 50 (Torr) 38 37 36 35 34 33 32- 31 30 O 4° OD Storz 2007 J Mamm 88, 24-31 500 1000 1500 2000 2500 Altitude (m) 3000 3500

The figure at right shows hemoglobin P50 values for populations of deermice collected at different altitudes, from sea level (0 m) to ~3,000 m. Based on this figure... A. Deermice collected at higher altitudes have higher blood O₂ binding affinity B. Deermice collected at lower altitudes have higher blood O₂ carrying capacity C. Deermice collected at lower altitudes have higher blood O₂ binding affinity D. Deermice collected at higher altitudes have lower blood O₂ carrying capacity E. None of the above P 50 (Torr) 38 37 36 35 34 33 32- 31 30 O 4° OD Storz 2007 J Mamm 88, 24-31 500 1000 1500 2000 2500 Altitude (m) 3000 3500

Basic Clinical Lab Competencies for Respiratory Care: An Integrated Approach

5th Edition

ISBN:9781285244662

Author:White

Publisher:White

Chapter9: Hemodynamic Monitoring

Section: Chapter Questions

Problem 2SEPT

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The figure at right shows hemoglobin P50 values for populations of deermice collected at different altitudes, from sea level (0 m) to ~3,000 m. Based on this figure... A. Deermice collected at higher altitudes have higher blood O₂ binding affinity Deermice collected at lower altitudes have higher blood O₂ carrying capacity B. C. Deermice collected at lower altitudes have higher blood O₂ binding affinity D. Deermice collected at higher altitudes have lower blood O2 carrying capacity E. None of the above P50 (Torr) 38- 37 - 36 35 - 34 33 32- 31 30 0 D 80 500 1000 Storz 2007 J Mamm 88, 24-31 1500 2000 Altitude (m) 2500 T 3000 3500
When YO2 = 0.5, the value of pO2 is defined as _______ (see the graph in Model 1).
Which is/are false? a. Carbaminohemoglobin is hemoglobin bound to carbon dioxide b. In the lungs, the oxyhemoglobin saturation curve undergoes a 'left shift' c. At a PO2 of 10 mmHg, there is more deoxyhemoglobin in blood that oxyhemoglobin d. Higher temperatures and lower pH cause hemoglobin to bind more readily with oxygen than in conditions of lower temperatures and higher pH
Hemoglobin poz in lungs tissues (4,500 m) po2 in lungs (sea level) po2 in 8. Lack of 2,3-BPG can be deadly. 1.0 BPG = 0 mM 38% A) What is 2,3-BPG? How is it produced and why does hemoglobin need 2,3- 30% ВPG? 37%- Y 0.5 B) Under what physiological conditions are blood levels of 2,3-BPG elevated? C) How does an increased level of 2,3-BPG help our bodies compensate through crises of a low availability of external oxygen? Highlight the action of 2,3-BPG on hemoglobin in your answer. BPG - 5 mM at sea level BPG 8 mM at high altitudes (4,500 m) 4 8 12 16 pO2 (kPa) Figure 5-17 Lehninger Principles of Biochemistry, Seventh Edition O 2017 W. H. Freeman and Company
(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…
The graph below shows the O₂-binding curves for myoglobin (Mb) and hemoglobin (Hb). a. 100 80 60 40 20 0 0 20 40 60 80 100 pO₂ (torr) a. Use the graph to determine the Kd of myoglobin for O₂ (show your approach). Write that in the provided space. b. What is the difference between myoglobin and hemoglobin that cause the O₂- binding curves to so be different? Answer in the provided space. c. Why is it important that hemoglobin has these particular O₂-binding characteristics? Answer in the provided space. YO₂
In mammals, the developing fetus obtains O₂ from its mother's blood via the placenta. For this to occur... A. The fetal hemoglobin must have a higher Pso than the maternal hemoglobin B. The O₂ equilibrium curve of the fetal hemoglobin must be left-shifted with respect to the curve for the maternal hemoglobin C. The maternal hemoglobin must have a higher O₂ binding affinity than the fetal hemoglobin D. The O₂ carrying capacity of the fetal hemoglobin must be greater than that of the maternal hemoglobin E. None of the above
1. The diagram on the right compares the O2 binding prop- 1.0 r erties of normal adult hemoglobin (HbA) to those of one dubbed Hb Great-Lakes characterized by the mutation Leu(B68)His. In the dia- gram Y= fraction of heme groups with bound O2, and pO2, the par- tial pressure of O2 above the solution, is measured in units of torr or mmHg. Hb Great Lakes 0.8 Hb A 0.6 Draw the corresponding Hill plot, being careful to reproduce graph- ically the dissociation equilibrium constant for O2 binding (Ko2) for Y each hemoglobin and to show the difference in the extent of allo- stery or cooperativity of subunit interaction in each type of hemo- globin. 0.4 You need draw only the central, linear portion of the Hill plot. 0.2 State what is the likely magnitude of the Hill constant (nH) for HbA from your reading and state what is the likely range of the magni- tude of the Hill coefficient for Hb Great Lakes. 0 10 20 30 40 50 60 pO2 (torr)
Which of the following is incorrect about 2,3-bisphosphoglycerate (BPG)? It is highly (-) charged b. It prevents binding of O₂ to hemoglobin Oc. It binds only to the relaxed (oxy) conformation of hemoglobin Od. It binds in the space between the four subunits of hemoglobin a.
The FIGURE 1 below shows the Bohr shift occurs in fetal haemoglobin (P and Q) and for maternal haemoglobin (R and S). 100 90 80 P pH 7.6, Q pH 7.4 70 60 R pH 7.6 -S pH 7.4 50 40 30 20 10 20 40 60 80 100 120 Po,(mm Hg) FIGURE 1 a) Define Bohr shift. State the effect of Bohr shift on the oxygen dissociation curve. b) Compare the oxygen dissociation curve for fetal and maternal haemoglobin. Explain. c) What happens to the oxygen dissociation curves when the pH is lowered? Explain. d) Give TWO reasons why an expectant mother is advised to give up the smoking. e) Sketch the curve for fetal myoglobin at pH 7.6. Label the curve as X. Percent O2 saturation of hemoglobin
Which of the following situations occurs if a person's blood becomes more alkaline? A. Hemoglobin molecules retain less oxygen per heme group under alkaline conditions than they do at neutral pH or under acidic conditions. B. Hemoglobin molecules give up oxygen more readily under alkaline conditions than they do under neutral pH or under acidic conditions. C. Hemoglobin molecules change shape and begin to lose oxygen molecules. D. Hemoglobin molecules retain oxygen more readily under alkaline conditions than they do at neutral pH or under acidic conditions. E. There is no change in hemoglobin's oxygen-binding affinity under alkaline conditions when compared to blood at neutral pH or under acidic conditions.
Which of the following is incorrect about hemoglobin? a. The binding of O₂ to one subunit decreases the O2-binding affinity of the other subunits Ob. It has two quaternary structures called the T (tense) and the R (relaxed) states O c. It displays cooperativity Od. It undergoes conformational changes upon binding 0₂