2,3-bisphosphoglycerate (BPG) is a negative allosteric regulator of hemoglobin that is produced red blood cells. Normally, red blood cell levels of BPG are 5 mmol/L, yielding curve 2. Individuals acclimated to high altitudes can have BPG levels of 8 mmol/L to optimize their oxygen utilization. 1 2 3 AS Por (mm Hg) Which curve represents hemoglobin of someone living at normal altitudes? 01 2 3 None of the answers are correct 2 and 3
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- Lycopene, which is abundant in tomatoes, is thought to have a potential benefit in protecting against many types of cancers. In the study, the results of which are shown in the Figure, mice were exposed to tobacco smoke or normal air. The amount of lung tissue damage caused by each exposure was measured in mice that were given tomato juice (1) or water (2). To estimate the destruction of the alveolar wall, a destructive index (DI) was calculated from histological slides of the lung. All lungs will show some level of damage, but a DI above 10% is considered significant destruction. What is the effect of tobacco smoke on the lung tissue in these mice? Source: Based on S. Kasagi et al. 2006. Tomato juice prevents senescence-accelerated mouse P1 strain from developing emphysema induced by chronic exposure to tobacco smoke. American Journal of PhysiologyLung Cellular and Molecular Physiology 290:L396L404.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?Suppose you visit the Dalai Lama in Dharamsala, India (elevation 1460 m),and you begin to ponder the “big questions,” such as “What is the fractionalsaturation of the Dalai Lama’s hemoglobin?”(a) Assuming the Dalai Lama’s hemoglobin has a Hill coefficient = 3.2,and a P50 = 31 mm Hg, calculate the change in fractional O2 saturationof his hemoglobin going from his lungs (where PO2 = 85 mm Hg) to hiscapillaries (where PO2 = 25 mm Hg).(b) Why do you suppose the Dalai Lama’s hemoglobin has a P50 higher thannormal (where “normal” = 27 mm Hg)?
- Suppose you visit the Dalai Lama in Dharamsala, India (elevation 1460 m), and you begin to ponder the “big questions,” such as “What is the fractional saturation of the Dalai Lama’s hemoglobin?” a) Assuming the Dalai Lama’s hemoglobin has a Hill coefficient = 3.2, and a P50 = 31 mmHg, calculate the change in fractional O2 saturation of his hemoglobin going from his lungs (where PO2 = 85 mmHg) to his capillaries (where PO2 = 25 mmHg). b) Why do you suppose the Dalai Lama’s hemoglobin has a P50 higher than normal (where “normal” = 27 mmHg)?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 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 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 answerDuring 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 lungsThe oxyhemoglobin dissociation (saturation) curve shifts to the right as the blood becomes more acidic. Under these conditions answer the following. At a P O2 = 40 mmHg the percent saturation of hemoglobin __________ and the content of oxygen bound to hemoglobin ____________. A. Decreases; decreases B. Increases; increases C. Increases; decreases D. Decreases; increases E. Does not change; does not change
- At a pO 2 of ~100 torr, hemoglobin in whole blood is about 90% saturated with oxygen. This corresponds to ______________ pressure, where the ____________ of hemoglobin is favored.Referring to the loading and unloading of oxygen from hemoglobin (as illustrated in the figure), which of the following statements is correct? Oxygen Dissociation Curve.png Group of answer choices When a person in ventilating at rest, 75% of hemoglobin is still oxyhemoglobin The percent saturation of hemoglobin is higher at higher partial pressures of oxygen A decrease in the pH of the blood would promote unloading oxygen from the hemoglobin All of these are correctIncreasing 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 function