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- 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…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: %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
- 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 saturationTo 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 decreasedFrom 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
- Below is an oxygen-binding curve for two hemoglobin variants. 1.0 0.8 0.6 B 0.4 0.2 20 40 60 80 100 O2 pressure (torr) Determine the p50 for variant A to the nearest 5 torr (i.e., if the p50 was 12, you would write 10). Determine the fraction of the hemoglobin B bound with O2 in the lungs (pO2 = 100 torr) that delivers oxygen to the tissues (pO2 = 20 torr)? Answer to the nearest 0.05 value (for example, 0.10 or 0.15). Which hemoglobin variant (write A or B or same) delivers more oxygen to tissues? Fraction bound with O2Figure 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.(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…
- Precise data have been obtained for the oxygen binding of stripped human hemoglobin at 25 °C: Poz (mm Hg) Poz (= 100 x Yo,) (mm Hg) % Saturation % Saturation (= 100 × Y) 0.10 0.315 5.75 76.0 0.350 0.990 7.94 90.9 0.794 3.06 12.88 96.9 1.748 9.09 29.51 99.0 2.884 24.0 67.60 99.7 4.467 50.0Help me pleaseArrange the following according to decreasing oxygen requirement. 1. crab 2. shark 3. clown fish 4. perch 5. hake Select one: O 12345 O 34512 O 54321 O 21543