Below is the reaction catalyzed by carbonic anhydrase. Please answer the following questions. CO₂ + H₂O → H+ + HCO3 a. The forward reaction is favored in the lungs b. When protons decrease the pH [Select] [Select] state is favored C. CO₂ acts directly as a [Select] hemoglobin by reacting to form carbonic and the allosteric effector of
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![Below is the reaction catalyzed by carbonic anhydrase. Please answer the following
questions.
CO₂ + H₂O → H+ + HCO3*
a. The forward reaction is favored in the lungs
b.
When protons decrease the pH [Select]
[Select]
c. CO₂ acts directly as a
[Select]
hemoglobin by reacting to form carbonic
Answer 1:
lungs
Answer 2:
decreases
Answer 3:
HbR
Answer 4:
negative heterotrophic
state is favored
Answer 5:
and the
allosteric effector of
reacting to generate protons another allosteric effector that stabilizes the T state](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fa6c5565a-787b-43d3-b23e-780453faf6da%2F6f1428de-7a3c-466e-9748-49db5af837d5%2Fjh2w75_processed.png&w=3840&q=75)
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- 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 saturationBelow 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…The illustration below shows several oxygen-dissociation curves. Assume that curve 3 corresponds to hemoglobin with physiological concentrations of CO2 and 2,3-BPG at pH 7. Which curves represent each of the following perturbations? Saturation (Y) N P⁰₂ Loss of quaternary structure. Increase in 2,3-BPG Decrease in CO₂ 1. 1 2. 2 3. 3 4. 4
- d) Determine which statements apply to hemoglobin, myoglobin, or neither (you can write in the corresponding numbers for each statement, as appropriate) Hemoglobin Myoglobin Neither 1. Oxygen binds irreversibly to this molecule.2. This molecule has greater affinity for oxygen.3. The oxygen dissociation curve is sigmoidal in shape.4. Carbon monoxide binds at an allosteric site, lowering oxygen binding affinity.5. The binding pattern for this molecule is considered cooperative.6. This molecule delivers oxygen more efficiently to tissues.7. As oxygen binds to this molecule, the shape of the molecule changes, enhancing further oxygen binding.8. The oxygen dissociation curve is hyperbolic in shape.Brown induration of the lungs H&E staining, Perls reaction Mark the corresponding elements in the picture: A - H&E staining B - Perls reaction 1 - intraalveolar hemosiderin 2 - interstitial hemosiderin 3- alveolar lumen 4 - thickened, sclerosed alveolar walls Description: Perls's reaction isTo demonstrate an understanding of oxyhemoglobin binding, insert a word from the list in each blank to complete the statements. Not all terms will be used. increased A right shift of the oxy-hemoglobin curve signifies a affinity for oxygen. hold acidic A temperature will cause a right shift of the oxy- hemoglobin curve. basic A more pH than normal blood pH will cause a right shift higher of the oxy-hemoglobin curve. As a person exercises, their muscles give off heat which raises the temperature of the blood. This will cause hemoglobin to more oxygen at the cells. lower release decreased
- Referring to the reaction catalyzed by carbonic anhydrase, explain via levels of reactants/products of this reaction, what happens when someone hyperventilatesDescribe what happens to respiratory rate when metabolic rate increases (which simulates metabolic acidosis). Explain how this compensation mechanism helps with metabolic acidosis (make sure you describe the relationship between pH, H+, and PCO2).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.
- A The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding oxygen to hemoglobin would be altered by the change in conditions noted. 2. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 poz pO2Crocodiles can use virtually 100% of the oxygen in its blood, whereas humans can extract only about 65% of the oxygen in their blood. Crocodile hemoglobin (Hb) binds HCO3, rather than 2,3-bisphosphoglycerate (BPG), when in the T-state. Which of the following best explains why HCO3¯ in the crocodile works better than 2,3-BPG in humans to help the Hb to release more of its bound oxygen? Crocodile Hb binds more oxygen than human Hb, and so the crocodile has more oxygen available than humans do. The [HCO3] varies with the amount of oxygen used, whereas the [BPG] in human erythrocytes is constant regardless of need. Humans require their hemoglobin to be sensitive to [BPG] in order for HbF (fetal Hb) to have a higher affinity for oxygen than maternal Hb. Since crocodile Hb binds HCO3, the HCO3 will not be available to bind to H+ (Bohr protons), and so more oxygen will be released to the tissues. Crocodiles are cold-blooded and so do not need as much oxygen as humans; this is why they can…A patient was connected an artificial ventilation device during a surgery on the gastrointestinal tract. 60 minutes after the start of the operation, a gas composition of the blood and pH were examined: - PaCO₂ = 26 mm Hg - pH = 7.5 Questions: 1. Give an opinion on the gas composition of blood and the acid-base state 2. What type of violation of external respiration is developed in the patient? 3. Give a definition of this type of respiratory pathology
