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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- Heart and muscle cells, where myoglobin resides, maintains an intracellular pO2 of about 2.5 torr. Calculate the fractional saturation (for human myoglobin) if a small change (1 torr) in oxygen partial pressure occurs in either direction (ie what happens at 1.5 torr, what happens at 3.5 torr?) and explain how a small change in oxygen pressure dramatically changes the myoglobin oxygen binding.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?p02 Y O2 (mmHg) 0.5 0.161 1 0.277 0.434 3 0.535 4. 0.605 0.697 0.754 12 0.821 20 0.885 Using the data provided in the table, the estimated p50 for myoglobin is mmHg and the fraction saturation of myoglobin at 30mmHg is 6
- 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?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?Below is the oxygen saturation curve for myoglobin and hemoglobin at a pH of 7. The p50 for myoglobin is indicated by the dashed lines on the graph. Mb and Hb O2 saturation: pH 7 10 0.8 Myoglobin 0.6 P50 = 0.2 0.4 Hemoglobin 0.2 - 0.0 pO2 [kPa] Which of these molecules (Mb/Hb/neither or both) has cooperativity? [ Select ] What would you expect to happen to the p50 of myoglobin if the pH were decreased to a pH of 4? [ Select ] Fraction saturation
- 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 oxygen transported to the mitochondria of muscle cells by myoglobin (KD = 2 torr). A new oxygen transport protein that exhibits cooperative binding has been isolated and is being studied in the lab. Calculate the Ko value if Y = 0.76 when pO₂2 = 18 torr (assume n = 2.5). How does this compare to the K₂ value for hemoglobin? Does this protein bind more or less tightly to oxygen compared to hemoglobin?A forearm skeletal muscle has a hemoglobin concentration of 92 microM. An arterial occlusion of the upper arm determines a decrease in saturation at a rate of 15% per minute, and no change in blood volume. Find the muscle oxygen consumption in units of micromolo2/(100 mltissue-min).Which of the following statements does NOT apply to the K value in the equation for the oxygen binding curve of myoglobin? It is numerically equal to p50. O A. It is defined as that oxygen partial pressure at which half of the oxygen binding sites are occupied. В. If Y> K, then myoglobin is less than 50% saturated with oxygen. OC. O D. It is a measure of the affinity of myoglobin for oxygen. OE. It is the value of po2 at which Y = 0.5.
- Although HbS binds O2 it becomes deoxygenated faster than HbA and doesn't deliver as much O2 to the peripheral tissues. 100 80 75 HbA 60 Black line shows normal O2 50 A K dissociation curve for HbA 40 В 0구 3.5 10 13.3 Oxygen tension (kPa) Q4: 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. 20 SaO2 (%)Please explain the difference between the oxygen dissociation curve created by myoglobin (asymptotic) versus the oxygen dissociation curve created by hemoglobin (sigmoidal). Why does this occur? Myoglobin O₂ saturation (%) 100 80 60 40 20 0 20 Hemoglobin 40 60 80 100 120 Po₂ (mmHg)A patient carrying a mutant form of hemoglobin (KD = 48 torr) is planning to take part in a hiking trip that involves strenuous physical activity at ~10,000 feet above sea level. The mutant hemoglobin has reduced oxygen binding cooperativity (n = 2.2) and displays no major structural abnormalities. a. Calculate the percent saturation of hemoglobin in the lungs (pO2 = 70 torr at this elevation) for this patient and for an individual carrying a normal version of hemoglobin b. Calculate the percent saturation of hemoglobin in active skeletal muscle tissue (pO2 = 15 torr) for this patient and for an individual carrying a normal version of hemoglobin c. Will this patient transport oxygen from the lungs to active muscle tissues more or less efficientlythan an individual with a normal version of hemoglobin on this trip? Briefly explain your answer