1, 2,3 or 4 for each prompt? PrTerOR1W+53.69%4 PointsThe image below shows several oxygen binding curves for haemoglobin. Assuming that curve number 3 represents haemoglobin aphysiological concentrations of CO2 and 2,3-bisphosphoglycerate, match the following changes to the curve that would be expectedSaturation (Y)1234Prompts①An increase in the concentration of CO₂AnswersSelect matchA decrease in the concentration of 2.3-bisphosphoglyencate3A decrease in pHSelect matchSelect matchSelect matchLoss of quaternary structureLast saved 10:26:12Questions Filter (16) ▼Q Searchpo₂K First< PreviousNext >Last >Chp

Prompt 1: Increase in CO2 The rightward shift observed in Curve 4 is associated to increase in CO2…

Answered: Pr Ter OR1W +53.69% 4 Points The image…

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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13. There are several ways to measure cellular respiration experimentally. For example, CO2 and O2 gas sensors measure changes over time in the concentration of carbon dioxide or oxygen, respectively. Design two experiments to test the effects of changing two different variables or conditions (one per experiment) on the respiration of research organism of your choice.
Below is a fractional saturation curve for O₂ binding to adult hemoglobin. Assume that curve Y represents a condition at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve X represents a condition that Fractional saturation (0) 0.2 0.0 0 Tissue PO, (kPa) 12 Lungs
Below is the equation that represents O2 binding to hemoglobin. Hb+4O2⇌Hb(O2)According to Le Chatelier’s principle, which form of the hemoglobin (Hb or Hb(O2)4) is predominant in the lungs where the partial pressure of oxygen is high? Explain. I need help answering this
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 (%)
Anadult mouse has a respiratory rate of∼163 breaths/min and a tidal volumeof∼0.15 ml at BTP (37 ◦C) [36]. The averageO2 consumption for one strainof male adult mice is 45.5 ml O2/hour at STP. For the inspired aircomposition shown in Table 7.7, compute the expired air composition. Youmay assume that the ratio of CO2 production/O2 consumption is the samefor humans and mice
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.
The O2-binding curves for normal haemoglobin (Hb A) and a mutant haemoglobin (Hb Kempsey) are shown in the diagram. Which of the following statements, based on this graph, are true? 1.0 0.8 Hb/Kempsey 0.6 Hb A 0.4 0.2 0.0 20 40 60 80 100 p02 (torr) 1. Hb Kempsey has a higher affinity for O, than HbA 2. Hb Kempsey is unable to transition between the R and T states 3. Hb Kempsey demonstrates cooperative binding of oxygen. 4. Hb Kempsey's curve could be explained by a loss of nearly all the cooperative interactions between the subunits. 5. A possible explanation for the curve observed with Hb Kempsey is mutation at His HC3. 2,4,5. O 1.2,5. O 1,2,3,4,5. O 2,3,4. O 1.2.4. Y (Fraction Saturation)
Below is the O₂ binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). Fraction of Hb bound with Oxygen 1.0 0.8 0.6 0.4 0.2 0.0 0 20 40 pO2 (torr) 60 80 ABC c. Which curve lacks cooperativity? [Select] Hb 100 a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no other small allosteric molecules associated)? [Select] b. Which curve has the lowest affinity (as measured by the p50)? [Select]
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.
Name 3 conditions (ex: pO2) in which the oxygen dissociation curve will shift to the left. Additionally, when there is such a shift to the left, does that mean that hemoglobin's affinity for O2 has increased or decreased?
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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

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