[ANIMAL PHYSIOLOGY] Which of the following statements about the oxygen-binding curves is FALSE? Select one: The PO2 and hemoglobin dissociation curve for myoglobin is to the left of fetal hemoglobin. O b. During high metabolic activity the PO2 and hemoglobin dissociation curve would be expected to shift to the left of normal. The blood returning to the lungs is still 75% saturated with oxygen. d. During normal activity (not exercising) the blood PO2 rarely falls below 40 mmHg. Oe. A larger decrease in PO2 is needed for hemoglobin to drop from 100% to 75% 02 capacity than from 75% to 50% 02 capacity.
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Which of the following statements about the oxygen-binding curves is FALSE?
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- Myoglobin benefits muscle cells by ... A. binding with O2 just as strongly as hemoglobin does. B. releasing bound O2 at lower PO2 conditions than hemoglobin does. C. increasing the effectiveness of fast glycolytic muscle fibers used in short bursts. D. contributing to the elasticity of flight muscle in birds. E. using hemoglobin as a reserve source of oxygen.1. Is this statement correct or incorrect? Explain. 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. 2. Is this statement correct or incorrect? Explain. Compared to hemoglobin, myoglobin has a lower binding affinity for O2 and a higher O2 binding capacity, two characteristics that allow myoglobin to efficiently provide skeletal muscle cells with a readily-accessible reservoir of O2.What is the biophysical reason that myoglobin (as opposed to hemoglobin) could never play the role of the oxygen transport system in the human body? 1. It binds oxygen too tightly 2. It binds oxygen too weakly 3. It binds oxygen too slowly 4. It does not bind oxygen cooperatively
- 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?Suggest a way in which the difference between the functions of hemoglobin and myoglobin is reflected in the shapes of their respective oxygen-binding curves.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 muscles
- a) How much more O2 can be transported by the blood when erythrocytesleave the lungs? Consider that a normal adult has a concentration of 15 g hemoglobin/100 mL of bloodand that the hemoglobin is 98% saturated with O2 at the usual pO2 of 100 torr in the lung at sea level. b) On the basis of the graph, explain how myoglobin facilitates the diffusion of O2 through muscle cells. Would myoglobin be effective as an O2-transport protein in cells of other tissues? Explain.As the value of p50 myoglobin for oxygen rises, it falls, rises, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls None of the aforementioned have a K _—- value, resulting in a strong affinity.In aerobic respiration, does inhaled molecular oxygen (O2) combine chemically with carbon to produce CO2? If so, explain when this occurs. If not, describe the fate of O2 and the production of CO2.
- 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 vivoPeople have been known to do things to increase the amount of hemoglobin, the oxygen transport molecule, in their bloodstream. From a cell's point of view, what would be the advantage of increased oxygen levels during intense exercise?Myoglobin ... A. has higher affinity for O2 than hemoglobin does. B. consists of four polypeptide chains, just as hemoglobin does. C. has a lower affinity for O2 than hemoglobin does. D. is found in the interstitial fluids, in contrast to hemoglobin that is found in red blood cells. E. can bind four O2 molecules at once.