Below 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 T T 0 20 40 pO2 (torr) 60 80 B Hb C c. Which curve lacks cooperativity? [Select] 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]
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- Below is the O2 binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). A Hb 20 40 60 80 100 pO2 (torr) 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 p5o)? [ Select ] c. Which curve lacks cooperativity? [ Select ] Fraction of Hb bound with Oxygen 0.2 0.4 0.6 0.8 0'0 >This graph shows the O2 binding curves of Hemoglobin. Which one is the R-state curve, and which one is the T-state? Why these curves are different comparing to the normal curve (middle one) 1.0 0.8 Observed hemoglobin- binding curve 0.6 0.4 0.2 0.0 50 100 150 200 p02 (torr) Y (fractional saturation)The 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)
- 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 LungsStudies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y (a2 y2), whereas maternal erythrocytes contains HbA (a2 B2). 1.0 HbF +BPG e 0.5 HbA +ВPG 2 4 6 8 10 pO2 (kPa) What is the physiological significance of the different O2 affinities?Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y (a2 y2), whereas maternal erythrocytes contains HbA (a2 B2). 1.0 ·HbF +BPG 0.5 HbA +ВPG 2 4 6 8 10 pO2 (kPa) Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain. b. What is the physiological significance of the different O2 affinities?
- A patient carrying a mutant form of hemoglobin (KD = 48 torr) is planning to take part in a hiking trip that involves strenuous physical activity at ~10,000 feet above sea level. The mutant hemoglobin has reduced oxygen binding cooperativity (n = 2.2) and displays no major structural abnormalities. a. Calculate the percent saturation of hemoglobin in the lungs (pO2 = 70 torr at this elevation) for this patient and for an individual carrying a normal version of hemoglobin b. Calculate the percent saturation of hemoglobin in active skeletal muscle tissue (pO2 = 15 torr) for this patient and for an individual carrying a normal version of hemoglobin c. Will this patient transport oxygen from the lungs to active muscle tissues more or less efficientlythan an individual with a normal version of hemoglobin on this trip? Briefly explain your answerwhich of adult haemoglobin or foetal haemoglobin will have a lower P50 value for binding O2. Be sure to define the term P50 and mention at a molecular level what interactions and structure differences are contribute to the observed values.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 O2
- 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 Company2,3-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 3Select the hemoglobin variant(s) that are described by each statement. (a) The variant least likely to cause pathological symptoms. (b) The variant(s) likely to show pl values different from that of HbA on an isoelectric focusing gel. (c) The variant most likely to show a decrease in BPG binding and an increase in the overall affinity of the hemoglobin for oxygen. Answer Bank Hb Milwaukee Hb Cowtown Hb Memphis Hb Philly Hb Providence Hb Bibba HbS