Hemoglobin S homozygotes who are severely anemic often have elevated levels of 2,3-bisphosphoglycerate (BPG) in their erythrocytes. Is this a beneficial effect? Yes, unless the person homozygous for HbS is pregnant. It might be initially beneficial, since the increased [BPG] will help to deliver more oxygen to the tissues. No, since the increased [BPG] will cause more sickling. This effect is neither beneficial nor harmful: BPG has nothing to do with sickle cell anemia. No, since the increased [BPG] decrease the hydrophobicity of the red blood cell making it more difficult for oxygen to diffuse into the cell.
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- The presence of 2,3-diphosphoglycerate (DPG) shifts the oxygen-hemoglobin dissociation curve right, why would you expect to find more DPG in the blood of a pregnant womanIncreasing concentrations of either 2,3-bisphosphoglycerate (BPG) or protons (H +) cause a ____________ ( rightward OR leftward) shift of the hemoglobin/oxygen binding curve. However, the mechanisms by which these two substances mediate this effect are distinct. Compare & contrast the way by which BPG and protons interact with hemoglobin and thereby influence its structure and functionUnder 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?
- The PO2 of placental blood is about 40 mmHg. What are the O2 saturations of maternal and fetal hemoglobin at this PO2?Briefly explain why fetal Hb has a higher affinity for O2 when compared to the adult Hb under similar condition of pH and [BPG].a) How does the fetal hemoglobin differ from the maternal hemoglobin in regards to structure and function? b) Explain the Bohr effect by drawing oxygen dissociation curves on a single graph that highlight changes in the hemoglobin affinity for O2 c) Describe the molecular basis of sickle cell anemia. Be specific
- Fetal hemoglobin binds 2,3 BPG with greater affinity than adult hemoglobin.TrueFalseDONT ANSWER THE FIRST TWO, JUST THE LAST ONEStudies 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…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…
- 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.In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.The primary allosteric regulator of hemoglobin oxygen affinity is ( ) and functions by stabilizing the ( ) state of enzyme.