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 is
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- Which are not allosteric effects that occur in hemoglobin? Are used by H* Involve binding away from the heme group Increase the Hill coefficient nH Reduce the affinity of heme for O2 Are used by DPGa.What is the difference between the 5th and 6 coordination sites in the heme group? b.What is the change of the oxygen dissociation curve represented by hemoglobin before and after dissociation into subunits? Briefly explain why.To 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
- P50 in Oxy-Hemoglobin dissociation curve represents That partial pressure(PaO2) of dissolved form at which Hb is 50% saturated with Oxygen50 mmHg difference between PAO2(alveolar) and PaO2(systemic)50% oxygen in dissolved form that ambient pressure at which PAO2(alveolar) is 50mmHgPaO2 of 50mmHgInternal respiration During internal respiration, the small amount of oxygen transported in dissolved plasma (1) quickly diffuses out of the plasma into interstitial fluid. Carbon dioxide diffuses into the blood and a small amount remains dissolved in the plasma (2). Most of the carbon dioxide continues into the red blood cell where some of it combines with hemoglobin (3) to form carbaminohemoglobin (4). Most carbon dioxide, however, combines with water (5) to form carbonic acid (6). This reaction is catalyzed by carbonic anhydrase. The carbonic acid then dissociates into hydrogen and bicarbonate ions (7). As bicarbonate ion concentration inside the red blood cell increases, bicarbonate ions diffuse out of the red blood cell into plasma (8) in exchange for chloride ions (9). Bicarbonate ions act as buffers within the plasma, controlling pH. Within the red blood cell, hydrogen ions (10) are buffered by hemoglobin (11). When hemoglobin binds hydrogen ions, it has a lower affinity for…Compare the three spectra. What can you observe when the starting hemoglobin is diluted? Does the position (λ) of the maximal absorption peaks change? Describe your observations.
- 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.Respiratory Concept Mapping Construct a map of gas transport using the following terms. You alveoli arterial blood carbaminohemoglobin carbonic anhydrase chloride shift dissolved CO₂ dissolved O₂ hemoglobin hemoglobin saturation oxyhemoglobin Po CO2 plasma 02 pressure gradient red blood cell venous bloodExplain how the binding of molecular oxygen (O2) to haemoglobin affects the tertiary structures of each monomer. Hence, explain how this influences the quaternary structure of the haemoglobin molecule, and how this helps haemoglobin to transport O2 from the lungs to the muscles.
- 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 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]Dipal mitoylphosphatidylcholine is the major component of surfactant, or surface active agent (an amphipathic molecule), that is secreted into lung alveoli to reduce the surface tension of the primarily aqueous extracellular fluid of the alveolar epithelia. Alveoli, also referred to as alveolar sacs, are the functional units of respiration. Oxygen and carbon dioxide diffuse across the walls of alveolar sacs, which are one cell thick. The water on alveolar surfaces has a high surface tension because of the attractive forces between the molecules. If the water’s surface tension is not reduced, the alveolar sac tends to collapse, making breathing extremely difficult. If premature infants lack sufficient surfactant, they are likely to die of suffocation. This condition is called respiratory distress syndrome. Draw the structure of dipalmitoylphosphatidylcholine. Considering the general structural features of phospholipids, propose a reason why surfactant is effective in reducing surface…
