The 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)
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- After spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the concentration of 2,3- bisphosphoglycerate (2,3-BPG) in red blood cells increases. What effect would an increased concentration of 2,3-BPG have on the oxygen-binding curve for hemoglobin? Why would this adaptation be beneficial for functioning well at high altitude?From the figure of O2 binding to myoglobin and hemoglobin (ignore the linemarked as T) as described in lecture (shown below) answer the following questions. a) Estimate the P50 for myoglobin from the plot. Show how this estimation isdetermined from the binding curve above. ( The first ghraph) b)Using YO2 = PO2/P50 + PO2 , calculate the fraction of O2 bound for myoglobin at 1 torr. (2nd graph) c)Using the binding curve on the previous page, show how you can estimate whatfraction of hemoglobin is bound near tissues at a pO2 of 30 torr and provide this value. If the pH were lowered, will the amount of O2 bound to hemoglobin at 30 torr increaseor decrease? Explain why this is so based on how this changes hemoglobin structure. If 2,3-BPG were added to the solution, will the amount of O2 bound to hemoglobin at30 torr increase or decrease? Explain why this is so based on how this changes hemoglobinstructure.Assume that during a 400-m running race, the pH decreases in muscle cells from 7.6 to 7.0 while the pO2 remains constant at 40 mm Hg. What is the effect on the oxygen binding of hemoglobin in the muscle cells? What is the implication of this? What is the effect on myoglobin?
- The dissociation constant is defined by p50 = 2.8 torr for myoglobin binding to oxygen. What is partial pressure of oxygen when half of the myoglobin proteins in solution are bound to oxygen?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 astructural variant of hemoglobin, HbF, consisting of two α and two γ subunits (α2 γ2 ), whereas maternal erythrocytes contain HbA (α2β2).(a) 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?(c) When all the BPG is carefully removed from samples of HbA and HbF, the measured O2 -saturation curves (and consequently the O2 affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2 -saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2 affinity of hemoglobin? How can the above information be used to explain the different O2 affinities of fetal and…In active muscle cells, the pO2 is about 10 torr at the cell surface and 1 torr at the mitochondria(the organelles where oxidative metabolism occurs). Calculate the percentage of bound oxygentransported to the mitochondria of muscle cells by myoglobin (KD = 2 torr).
- Studies of oxygen transport in pregnant mammals have shown 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 γ and two β subunits (γ2β2), whereas maternal erythrocytes contain HbA (α2β2). (a) 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? (c) When all the BPG is carefully removed from samples of HbA and HbF, the measured O2-saturation curves (and consequently the O2 affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2-saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2 affinity of hemoglobin? How can the above information be used to explain the different O2 affinities of…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 musclesConsidering the quantity of hemoglobin in an erythrocyte and the oxygen-binding properties of hemoglobin, calculate how many molecules of oxygen one erythrocyte could carry?
- A new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?3A.Describe the difference in biological func on of myoglobin and hemoglobin in the body. How does hemoglobin’s sigmoidal O2 binding curve contribute to its biological func on?( Think binding affinity) 3B. Describe the different ways in which the affinity of oxygen to hemoglobin can be modified in vivoYou want to measure the blood oxygen level in a drop of blood using a pulse oximetry device. If you have a light source at 700nm, and 1mm of path length. What must be the concentration of, a.Oxidized hemoglobin (HbO2) concentration in blood so that the light intensity at the output decreases to the one tenth of input intensity? b. Reduced hemoglobin (Hb) concentration in blood so that the light intensity at the output decreases to the one tenth of input intensity? c.At the concentration you found in b, what is Ii / If for oxidized hemoglobin?