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Which hemoglobin has a higher affinity for O2 at the tissue pO2 of around 4 kPa?
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- 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 Lungs(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 is the equation that represents O2 binding to hemoglobin. Hb+4O2⇌Hb(O2)According to Le Chatelier’s principle, which form of the hemoglobin (Hb or Hb(O2)4) is predominant in the lungs where the partial pressure of oxygen is high? Explain. I need help answering this
- 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 >Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?Under appropriate denaturing conditions, hemoglobin can dissociate into four separate subunits. An isolated alpha subunit binds oxygen, but the O2-saturation curve is hyperbolic rather than sigmoid. In addition, the binding of oxygen to an isolated alpha subunit is not affected by the presence of H+, CO2, or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?
- 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 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]which 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.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)
- 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)What are the effects of PO2 on carbaminohemoglobin formation and H1 binding by hemoglobin?Suppose you visit the Dalai Lama in Dharamsala, India (elevation 1460 m),and you begin to ponder the “big questions,” such as “What is the fractionalsaturation of the Dalai Lama’s hemoglobin?”(a) Assuming the Dalai Lama’s hemoglobin has a Hill coefficient = 3.2,and a P50 = 31 mm Hg, calculate the change in fractional O2 saturationof his hemoglobin going from his lungs (where PO2 = 85 mm Hg) to hiscapillaries (where PO2 = 25 mm Hg).(b) Why do you suppose the Dalai Lama’s hemoglobin has a P50 higher thannormal (where “normal” = 27 mm Hg)?