100 80 75 HbA 60 Black line shows normal O2 dissociation curve for HbA S 50 - A K 40 - В 20 - 3.5 10 13.3 Oxygen tension (kPa) 24: Using the curve as a guide, predict whether the oxygen binding curve is shifted to the left (A) or to the right (B) for HbS.
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- 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…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?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…
- Which hemoglobin has a higher affinity for O2 at the tissue pO2 of around 4 kPa?Which of the following statements about the oxygen-binding curves is FALSE?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? Explain
- What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.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 vivoXena lights a fire to keep warm, and cook his green root vegetables, which are extremely alkaline. Xena is so hungry, and she is eating all her green root vegetables making her blood quite alkaline for a short time. An example of the O2/Hb dissociation curve is provided below. The central blue line represents ‘normal blood’, and the typical affinity of Hb for O2. Referring to this figure will help you answer the following questions. Describe how the oxygen transporting capacity of haemoglobin will change for a short time in the presence of alkaline blood and explain the consequence of this change to the oxygen supply of peripheral tissues for this short time. Justify your answers.
- 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?Briefly explain how the respiratory exchange ratio is used to estimate which substrate is being utilized during exercise. What is meant by the term nonprotein R?Comparison of Fetal and Maternal Hemoglobins.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 oftwo a and two g subunits (α2γ2), 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 O2affinities) 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 O2affinity of hemoglobin? How can the above information be used…
