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. د C Normal Yakima pO2 (tor) 10 Yo2 Yoz 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
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- Determine the Hill coefficient, n, for myoglobin (Mb), hemoglobin (Hb), and recombinant hemoglobin (HbX). Given the results of the Hill plot and the dissociation curves, which of the following are true? Oxygen binding by HbX is less cooperative than for Hb The Hill coefficient for Hb is equal to the number of hemoglobin O2 binding sites Oxygen binding by Hb is less cooperative than for Mb. HbX will load less O2 in the lungs and unload less O2 in active tissues than normal Hb.In carbon monoxide (CO) poisoning, CO binds to hemoglobin, therebydecreasing the uptake of O2 by hemoglobin. In addition, when CO bindsto hemoglobin, the oxygen-hemoglobin dissociation curve shifts to theleft. How does this shift affect the ability of tissues to get O2? ExplainSuppose you visit the Dalai Lama in Dharamsala, India (elevation 1460 m), and you begin to ponder the “big questions,” such as “What is the fractional saturation of the Dalai Lama’s hemoglobin?” a) Assuming the Dalai Lama’s hemoglobin has a Hill coefficient = 3.2, and a P50 = 31 mmHg, calculate the change in fractional O2 saturation of his hemoglobin going from his lungs (where PO2 = 85 mmHg) to his capillaries (where PO2 = 25 mmHg). b) Why do you suppose the Dalai Lama’s hemoglobin has a P50 higher than normal (where “normal” = 27 mmHg)?
- Describe the effects of increased DPG on the oxygen–hemoglobin dissociation curve. What is the adaptive importance of the effect of DPG on the curve?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)?Which hemoglobin has a higher affinity for O2 at the tissue pO2 of around 4 kPa?
- Is the cooperative binding of oxygen by hemoglobin better described by the concerted or the sequential model?What is the molecular basis for the difference in the electrophoretic pattern between normal hemoglobin A and hemoglobin S?During strenuous exercise, the oxygen-hemoglobin dissociation curve shifts to the right. This rightward shift reflects an increase in the affinity of hemoglobin for oxygen and favors loading of O2 onto hemoglobin in the lungs
- The following graph shows partial saturation (Y) of myoglobin (Mb), adult hemoglobin (HbA) and fetal hemoglobin (HbF) as a function of partial oxygen pressure (in mmHg). Use it to answer the question: Fetal hemoglobin ( biological function: HbF) demonstrates lower p50 than adult hemoglobin (HbA). This adaptation has the following A. Allow fetal hemoglobin form pentamer subunits. B. HbF has lower affinity for for O2 compared to adult Hb C. Allow fetal hemoglobin to effectively intercept oxygen from mother's hemoglobin. D. Allow fetal hemoglobin to replace myoglobin in musclesWhy is it advantageous for the oxygen-hemoglobindissociation curve to shift to the left in the lungs and to theright in tissues?Considering the quantity of hemoglobin in an erythrocyte and the oxygen-binding properties of hemoglobin, calculate how many molecules of oxygen one erythrocyte could carry?