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 affinityDeermice collected at lower altitudes havehigher blood O₂ carrying capacityB.C. Deermice collected at lower altitudes havehigher blood O₂ binding affinityD. Deermice collected at higher altitudeshave lower blood O2 carrying capacityE. None of the aboveP50 (Torr)38-37 -3635 -343332-31300D805001000Storz 2007 J Mamm88, 24-311500 2000Altitude (m)2500T3000 3500

In the lungs, oxygen from the air we breathe diffuses into the blood. Blood has tremendous potential…

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 P50 (Torr) 38 37 36 35 34 33 32 31 30 to 08 00 500 1500 Altitude (m) 1000 Storz 2007 J Mamm 88, 24-31 2000 2500 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 P50 (Torr) 38 37 36 35 34 33 32 31 30 to 08 00 500 1500 Altitude (m) 1000 Storz 2007 J Mamm 88, 24-31 2000 2500 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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A. The affinity of oxygen to hemoglobin in Baguio City B. The affinity of oxygen to hemoglobin at sea level O A. The FIRST quantity is the larger of the 2. O B. The SECOND quantity is the larger of the 2. O C. The two quantities are EQUAL in size A. The rate at which O2 detaches from hemoglobin when temperature is high B. The rate at which O2 detaches from hemoglobin when temperature is low O A. The FIRST quantity is the larger of the 2. O B. The SECOND quantity is the larger of the 2. C. The two quantities are EQUAL in size
2,3-bisphosphoglycerate (BPG) is a negative allosteric regulator of hemoglobin that is produced in red blood cells. Normally, red blood cell levels of BPG are 5 mmol/L, yielding curve 2. Individuals acclimated to high altitudes can have BPG levels of 8 mmol/L to optimize their oxygen utilization. Saturation 2 3 S Which curve represents hemoglobin of someone living at normal altitudes? 1 2 Pos (mm Hg) 3 None of the answers are correct 2 and 3
Which of the following scenariosare correct?Select all that apply A. High levels of PCO2will cause loading of O2ontohemoglobin. B. An increase in pH will causeO2to unload from hemoglobin. C. High PO2levels will increase saturation of Hb with O2. D. An increase in bodytemperature will cause O2to unload from hemoglobin.
Calculate the hemoglobin concentration of an unknown sample given the following info: concentration of known = 12.5 g/dl; absorbance of unknown = 0.48; absorbance of known = 0.65 a. 16.9 g/dl b. 9.2 g/dl c. 8.7 g/dl d. 11.3 g/dl e. 10.4 g/dl
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…
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
From your graph, estimate the P50 for normal hemoglobin and the mutant corresponding to your student number and explain if these results support your expectations regarding the mutant's oxygen affinity compared to normal hemoglobin. ف C Normal Yakima pO2 (torr) Yo2 Yo2 10 0.05 0.10 15 0.10 0.25 20 0.25 0.45 25 0.50 0.70 30 0.75 0.85 40 0.85 0.95 60 0.95 0.98 H
(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…
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…
A The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding oxygen to hemoglobin would be altered by the change in conditions noted. 2. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 poz pO2
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)