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- Figure 5 shows oxyhemoglobin dissociatlon curves at pH 7.2 and pH 7.4. Which of the following is true at PO2 less than 40 mm Hg? 27. % saturation af haemogiobin 100 pH 7.4 80 60 pH 7.2 40 + 20 10 20 30 40 50 60 70 Po; (mm Hg) Figure 5 A. Hemoglobin retains less O2 at pH 7.4 compared to pH 7.2. B. Hemoglobin retains less O2 at pH 7.2 compared to pH 7.4. C. The release of O2 from hemoglobin is not influenced by the production of CO2. D. At pH 7.2 where CO2 production is less than pH 7.4, hemoglobin releases less O2.Figure 6 shows the binding of oxygen to myoglobin and haemoglobin (Y-axis: Fraction saturation) when they are exposed to various partial pressures of oxygen (X-axis: pO2). 0.9 0.8 Myoglobin 0.7 0.6 0.5 0.4 Hemoglobin 0.3 0.2 0.1 2 10 12 Po, (kPa) Figure 6 (i) Briefly compare the protein structure of myoglobin to that of haemoglobin. (ii) Based on Figure 6, explain the differences between the functions performed by myoglobin and haemoglobin. Fraction saturationBelow 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
- 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)Table 4: Presence or Absence of Agglutination Mother 1 Father 1 Child 1 Mother 2 Father 2 Child 2 Mother 3 Father 3 Child 3 Anti-A Sera Agglut No Agglut No No No Agglut No Agglut Anti-B Sera Agglut No No No Agglut Agglut No No No Anti-Rh Sera No Agglut Agglut Agglut No Agglut No No No Blood Type AB- O+ A+ 0+ B- B+ A- O- A-Blood in our body changes color as a function of its oxygenation state. Given the spectral data below, calculate the absorbance of red light (600 nm) of fully oxygenated and deoxygenated blood. Using this data, determine what percentage of red light would go through a sample of blood that is 50% oxygenated. Assume the patient has a hemoglobin concentration of 10 mM and pathlength of 1 cm.
- Calculate the average ml of oxygen molecules in 100 ml blood in the athletes at low altitude and then in athletes in high altitude while training at high altitude. Use the following information: 1.39 ml of oxygen per gram of hemoglobin. Do athletes training at high altitudes have more or less oxygen molecules per ml of blood then athletes training at low altitudes? Explain why this difference gives athletes who train at high altitudes an advantage over athletes who train only at low altitudes.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 decreasedIn 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.
- 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 correctWhat kind of Oxygen-Dissociation curve do you expect when carbon monoxide attaches to hemoglobin molecules ? ------------------------------------------- Why do we observe this change from a normal oxygen dissociation curve ? And why is this change hazardous ? Please Answer All Question, Don't Answer only One Question if you are real expert ! Don't Spam or copy from Other websites. It's Urgent Thankyou and All the Best :)Considering the quantity of hemoglobin in an erythrocyte and the oxygen-binding properties of hemoglobin, calculate how many molecules of oxygen one erythrocyte could carry?
