Which of these is the correct equation (not including energy sources or products) for CELLULAR RESPIRATION : 6C6H1206 + 602 -> 6CO2 + 6H2O C6H1206 + O2 -> CO2 + H2O C6H1206 + 602 -> 6CO2 + 6H2O 6H2O + 602 -> 6CO2 + C6H12O6
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- 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)2,3-bisphosphoglycerate (BPG) is a negative allosteric regulator of hemoglobin that is produced in red blood cells. Normally, red blood cell levels of BPG are 5 mmol/L, yielding curve 2. Individuals acclimated to high altitudes can have BPG levels of 8 mmol/L to optimize their oxygen utilization. Saturation 2 3 S Which curve represents hemoglobin of someone living at normal altitudes? 1 2 Pos (mm Hg) 3 None of the answers are correct 2 and 3Oxygen affinity of fetal blood is higher than that of maternal blood and may help to provide the fetus with an adequate oxygen supply during pregnancy. In mammals, 2, 3-biphosphosphoglycerate (BPG) mediates intracellular hemoglobin function by lowering cxygen affinity. Fetal red blood cells have higher affinity for oxygen because of a smaller effect of BPG on oxygen affinity of fetal hemoglobin (Hb F) compared with adult Hb (Hb A). Which symbol shows the PS0 value corresponding to Hb F? 14 12 10 0.0 0.5 1.0 1.5 2.0 2,3-BPG (mM) O Crcle O Dimond O Square O Triangle (6H ww) d
- 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 option best describes the following figure? Y (fraction saturation) 1.0 0.8 0.6 0.4 0.2 0.0 0 20 Oxygen Binding plot 40 60 p02 (torr) 80 100 A) Curve x = adult haemoglobin, curve y = fetal haemoglobin B) Curve x = myoglobin, curve y = haemoglobin C) Curve x = fetal haemoglobin, curve y = adult haemoglobin D) Curve x = fetal haemoglobin, curve y = myoglobin E) Curve x = adult haemoglobin, curve y - myoglobinBelow 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
- As the value of p50 myoglobin for oxygen rises, it falls, rises, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls, falls None of the aforementioned have a K _—- value, resulting in a strong affinity.Hemoglobin and myoglobin both use heme as their prosthetic group and they both bind O2. However, their O2-binding curves indicate these proteins have different activities. What lind of information can be learned about the differences between the curves?Which of the following statements regarding the transport of oxygen by hemoglobin is correct? Upon binding of oxygen to heme, a shift in the position of the distal His ultimately induces the switch from T to R states When fully bound to oxygen, AG(R-state)Discuss the regulation on respiration by explaining the picture below. Make it brief yet substantialWhich of the following is the correct chemical equation for aerobic respiration? O A) C6H1206 + 602 → 6CO2 + 6H2O B) C6H1206 + 6CO2 → 602 + 6H2O C) C6H1206 + 6O2 → 6CO2 + 602 D) 6CO2 + 6H2O → C6H1206 + 6O2As the value of p50 myoglobin for oxygen. increases, decreases decreases, increases decreases, decreases increases, increases None of the above the value of K _--_, resulting in a high affinity ofSEE MORE QUESTIONS