The illustration below shows several oxygen-dissociation curves. Assume that curve3 corresponds to hemoglobin with physiological concentrations of CO2 and 2,3-BPGat pH 7. Which curves represent each of the following perturbations?Saturation (Y)NP⁰₂Loss of quaternarystructure.Increase in 2,3-BPGDecrease in CO₂1. 12. 23. 34. 4

We know that hemoglobin (Hb) is the protein responsible for carrying O2 in blood. Certain other…

Answered: The illustration below shows several…

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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Similar questions

Describe three ways in which carbon dioxide can be transported.
Given the oxygen dissociation curves, which of the following statements are correct? Which residue in HbA β do you think contributes the most to the increased interaction between HbA aand 2,3‑BPG?
Measurements of oxygen binding by whok human blood, at 37 °C, at pH 7.4, and in the presence of 40 mm Hg of CO, and normal physiological lkvels of 2,3-BPG (5 mmol/L of cells), give the following: Po, (mm Hg) % Saturation (=100 x Yo) 10.6 10 19.5 30 27.4 50 37.5 70 50.4 85 77.3 96 92.3 98 (a) From these data, construct a binding curve, and estimate the percent oxygen saturation of blood at (1) 100 mm Hg, the approximate partial pressure of O, in the lungs, and (2) 30 mm Hg, the approximate partial pressure of Oz in venous blood. (b) Under these conditions, what percentage of the oxygen bound in the lungs is delivered to the tissues? (c) Using the data in Figure 7.27, repeat the calculation of part (b) if the pH drops to 6.8 in capillaries but goes back to 7.4 as CO, is unloaded in the lungs.
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 a study of O2 uptake by muscle at high altitude, a physiologist prepares an atmosphere consisting of 79 mole % N2, 17 mole % 16O2, and 4.0 mole % 18O2. (The isotope 18O will be measured to determine O2 uptake.) The total pressure is 0.75 atm to simulate high altitude. Calculate the mole fraction and partial pressure of 18O2 in the mixture.
What effect does hyperventilation have on blood pH and why? What simple measure can be used to correct the pH imbalance and how does it work? What effect would hyperventilation have on hemoglobin O2 saturation in a normal healthy individual? What effect would a PaO2 of 60 mmHg have on hemoglobin O2 saturation and why? (explain in terms of the O2-Hb dissociation curve)
Using the information below, calculate the Oxygen Diffusion Driving Force (mmHg), which is the pressure gradient that drives O₂ out of the alveoli and into the blood (calculated as PAO₂- PVO₂): Barometric Pressure at Salt Lake City, UT= 4,226 ft. (1,288 m)→→ 657 mmHg . Estimated mixed-venous PO2 of blood returning to the lungs after leaving the muscle (PvO₂) at rest, measured at Salt Lake City, UT: PvO2 = 36 mmHg O 90 mmHg O 54 mmHg O 36 mmHg O 29 mmHg
Oxygen-hemoglobin curve dissociation curve: Which various factors can determine the amount of saturation? why is this curve so steep? how ph and temperature affect it? how does the binding of oxygen molecules in bohr and haldane effect affect the 3d shape of hemoglobin and how does that have to do with the curve?
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
Messner and Habeler's 1978 ascent of Mount Everest without oxygen-breathing apparatus is often described as one of the most remarkable physical accomplishments achieved by humans. Table 1 shows respiratory gas and arterial pH values measured in a resting mountaineer at sea level, Everest base camp and Everest summit. Use the differences in these values to explain how breathing regulation changes when at rest at the 3 altitudes indicated. Calculations are not required but you may wish to consider the role of central and peripheral chemoreceptors and their relationship to paCO,, minute ventilation and alveolar pO, in your response. Table 1: Respiratory gas composition and arterial pH measured in a resting mountaineer at sea-level, Everest base-camp and Everest summit. Arterial Barometric Alveolar Inspíred p02 (FIO2) pO2 (PAO2) pCO2 (расо2) Altitude Pressure Arterial (m) pH mmHg mmHg mmHg mmHg Sea Level 760 150 106 36 7.4 Everest Base 5,400 404 75 51 20.4 7.6 Camp Everest 8,848 252 43 34…
Given: Under normal circumstances the partial pressure of oxygen in air is approximately 160 mmHg. Let’s assume in the alveoli it drops to 100 mmHg when a person breaths 12x per minute. At the end of a 1-mile sprint a person is breathing 60x per minute, but, due to the decrease in the amount of time each breath spends in the lungs, the oxygen partial pressure is only drops to 140 mmHg before exhalation. a. How much has the amount of oxygen diffused through the alveoli increased or decreased? (Answer part a )
Below are multiple oxygen binding affinity curves for hemoglobin. The affinity curve for normal hemoglobin in blood is represented by curve "D," at a pH of 7.2 and at a concentration of 5mM BPG and 26 mM CO2. O₂ saturation (%) 100 Answer 1: B Answer 2: [Select] Answer 3: B Answer 4: 80 A 60 1. How would changes to acidity, BPG concentration and CO₂ levels affect the binding affinity curve and p50? lower than Answer 5: E 40 1. BPG concentration is decreased to 3mM: The binding affinity curve would look like B. The p50 would be lower than normal (D). 2. pH is increased to 7.6: The binding affinity curve would look like B. The p50 would be [Select] normal (D). 20 3. CO₂ concentration is increased to 30 mM: The binding affinity curve would look like. [Select] The p50 would be Answer 6: 0 normal (D). II. The hemoglobin has been treated with a denaturing solution which disrupts quaternary structure only, and has a binding affinity resembling myoglobin. The binding affinity curve would look…

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