The following data describe the binding of oxygen to human myoglobin. Posygen (mm Hg) Percent Saturation 0.5 16.1 2.0 27.7 3.0 53.5 4.0 60.5 6.0 69.7 8.0 75.4 12.0 82.1 20.0 88.5 From these data the approximate P50 (mm Hg) value is: A. 1.0 В. 1.4 С. 1.9 D. 2.6 Е. 3.2 F. 3.5 G. 3.7 H. 3.9 I. 4.0
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- 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 50.0The following data describe the binding of oxygen to human myoglobin at 37 °C. Po, (mm Hg) Yo. Po, (mm Hg) Yo: 0.5 0.161 0.697 1 0.277 8. 0.754 2 0.434 12 0.821 3 0.535 20 0.885 0.605 From the se data, estimate (a) Pso and (b) the fraction saturation of myoglo- bin at 30 mm Hg, the partial pressure of Oz in venous blood. 4)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). 0.9 0.8 Myoglobin 0.7 0.6 0.5 0.4 Hemoglobin 0.3 0.2 0.1 2 10 12 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
- The arterial O₂ concentration is given by the following expression [0₂] = 0.003 P0₂ + (PO₂)².8 +(26) 2.8 1. ЗЧНЬ (Рог ) 2-8 Where Poz is the alveolar O₂ pressure and Hb is the hemoglobin concentration in g/dL, respectively A subject who is at 0-95 ATM (211-0₂) has an arterial O₂ concentration of 19ml/dL and and arterial CO₂ pressure of 38mm Hg. Also, VO₂ = 340mL/min.; VCD₂ = 289 mL/min. Therefore, your hemoglobine level is: A. 14.39 Idl 8. 14.8 g/dl C. 15.2 g/dl D. 15.7g/dL E. 16 g/dLp02 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 6Below 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 O2
- Below is a fractional saturation curve for O₂ binding to adult hemoglobin. Assume that curve Y represents a condition at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve X represents a condition that Fractional saturation (0) 0.2 0.0 0 Tissue PO, (kPa) 12 LungsVO2 calculation scenario: Body mass= 102 kg, HR= 180 beats/min, SV= 110 ml blood/beat, venous oxygen content = 4 ml O2/100 ml blood. What is the VO2 (ml O2/kg/min) for this scenario? (round to the nearest tenth). Remember your answer, as you will be asked to interpret this VO2 in another question. a. 31.1 b. 776.5 c. 3.5 d. 221.8 e. 7.8The O2-binding curves for normal haemoglobin (Hb A) and a mutant haemoglobin (Hb Kempsey) are shown in the diagram. Which of the following statements, based on this graph, are true? 1.0 0.8 Hb/Kempsey 0.6 Hb A 0.4 0.2 0.0 20 40 60 80 100 p02 (torr) 1. Hb Kempsey has a higher affinity for O, than HbA 2. Hb Kempsey is unable to transition between the R and T states 3. Hb Kempsey demonstrates cooperative binding of oxygen. 4. Hb Kempsey's curve could be explained by a loss of nearly all the cooperative interactions between the subunits. 5. A possible explanation for the curve observed with Hb Kempsey is mutation at His HC3. 2,4,5. O 1.2,5. O 1,2,3,4,5. O 2,3,4. O 1.2.4. Y (Fraction Saturation)
- 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 3Below 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 saturationBelow is the O₂ binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). Fraction of Hb bound with Oxygen 1.0 0.8 0.6 0.4 0.2 0.0 0 20 40 pO2 (torr) 60 80 ABC c. Which curve lacks cooperativity? [Select] Hb 100 a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no other small allosteric molecules associated)? [Select] b. Which curve has the lowest affinity (as measured by the p50)? [Select]
