Please proper Explain your answer Choose the correct answers based on the oxygen binding curves shown below forbeaver hemoglobin measured at two pH values. Assume that the blood leaving thelungs of the beaver has pO2 = 100 torr and pH = 7.6. Assume that after a beaver hasbeen busy building dams all day, the blood leaving the actively respiring muscletissue has pO2 = 20 torr and pH = 7.2.Beaver HemoglobinYO210.90.80.70.60.50.40.30.20.10020pH 7.64060p02 (torr)80pH 7.2100120Hb in the blood leaving the lungs is about 99% saturated with oxygen.Hb in the blood leaving actively respiring muscle tissue is about 10% saturatedwith oxygen.Based on the above curves, each mole of oxygen binding sites in Hb is deliveringabout 0.49 moles of oxygen from the lungs to the muscles.Hb in the blood leaving actively respiring muscle tissue is about 50% saturatedwith oxygen.OBased on the above curves, each mole of oxygen binding sites in Hb is deliveringabout 0.89 moles of oxygen from the lungs to the muscles.

The Bohr effect is defined as a phenomenon that describes the reduced affinity of hemoglobin for…

Choose the correct answers based on the oxygen binding curves shown below for beaver hemoglobin measured at two pH values. Assume that the blood leaving the lungs of the beaver has pO2 = 100 torr and pH = 7.6. Assume that after a beaver has been busy building dams all day, the blood leaving the actively respiring muscle tissue has pO2 = 20 torr and pH = 7.2. Beaver Hemoglobin YO2 1 0.9 0.8 0.7 0.6 0.5 0.4 0.3 0.2 0.1 0 0 20 pH 7.6 40 60 p02 (torr) 80 pH 7.2 100 120

Choose the correct answers based on the oxygen binding curves shown below for beaver hemoglobin measured at two pH values. Assume that the blood leaving the lungs of the beaver has pO2 = 100 torr and pH = 7.6. Assume that after a beaver has been busy building dams all day, the blood leaving the actively respiring muscle tissue has pO2 = 20 torr and pH = 7.2. Beaver Hemoglobin YO2 1 0.9 0.8 0.7 0.6 0.5 0.4 0.3 0.2 0.1 0 0 20 pH 7.6 40 60 p02 (torr) 80 pH 7.2 100 120

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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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: %
Figure 5 shows oxyhemoglobin dissociatlon curves at pH 7.2 and pH 7.4. Which of the following is true at PO2 less than 40 mm Hg? 27. % saturation af haemogiobin 100 pH 7.4 80 60 pH 7.2 40 + 20 10 20 30 40 50 60 70 Po; (mm Hg) Figure 5 A. Hemoglobin retains less O2 at pH 7.4 compared to pH 7.2. B. Hemoglobin retains less O2 at pH 7.2 compared to pH 7.4. C. The release of O2 from hemoglobin is not influenced by the production of CO2. D. At pH 7.2 where CO2 production is less than pH 7.4, hemoglobin releases less O2.
Below is the oxygen saturation curve for myoglobin and hemoglobin at a pH of 7. The p50 for myoglobin is indicated by the dashed lines on the graph. Mb and Hb O2 saturation: pH 7 10 0.8 Myoglobin 0.6 P50 = 0.2 0.4 Hemoglobin 0.2 - 0.0 pO2 [kPa] Which of these molecules (Mb/Hb/neither or both) has cooperativity? [ Select ] What would you expect to happen to the p50 of myoglobin if the pH were decreased to a pH of 4? [ Select ] Fraction saturation
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
To 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 decreased
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…
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-
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Which 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 uM
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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
p02 Y O2 (mmHg) 0.5 0.161 1 0.277 0.434 3 0.535 4. 0.605 0.697 0.754 12 0.821 20 0.885 Using the data provided in the table, the estimated p50 for myoglobin is mmHg and the fraction saturation of myoglobin at 30mmHg is 6