for normal hemoglobin in blood is represented by curve "D," at a pH concentration of 5mM BPG and 26 mM CO2. O₂ saturation (%) 100 80 A B 60 40 20 20 D E normal Hb 40 60 80 Po₂ (mmHg) 100 1. How would changes to acidity, BPG concentration and CO₂ levels a affinity curve and p50? 1. BPG concentration is decreased to 3mM: The binding affinity cur like B. The p50 would be lower than normal (D). 2. pH is increased to 7.6: The binding affinity curve would look like be [Select] normal (D).
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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 saturationCarbon dioxide is dissolved in blood (pH 7.5) to form a mixture of carbonic acid and bicarbonate. Part A Neglecting free CO2, what fraction will be present as carbonic acid? (pKa for H₂CO3 and HCO3 are 6.3 and 10.25, respectively) Express your answer using two significant figures. VE ΑΣΦ Submit Request Answer ?A 42 year old man is admitted to the hospital with the sudden onset of dyspnea with clear lungs and a normal chest xray. He has just been on a flight from Australia to New York City. The blood gas values are as follows: pH 7.56, pCO2 16, pO2 80, 95% saturation What is this person’s A-a gradient?
- If normal plasma pH is 7.4 and normal [CO2) is 1.2 mM, what is the normal (HCO321? The pK9 for this system is 6.1. Phosphoric acid (H3PO4) has three dissociable protons, with the pK,'s shown below. Which form of phosphoric acid predominates in a solution at pH 4? Explain your answer. Acid H3POA 2.14 H2PO4 6.86 HPO,2- 12.4A 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 answerBelow 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
- Exposure to air containing 600 ppm CO for 30 minutes results In an actual HbCO blood concentration of 10%. Estimate the percentage of the equilibrium saturation value of HbCO.O, saturation curve is shown beloww for hemoglobin at various pHs. Detail this Bohr effect from the molecular perspective. Be sure to include discussion of what causes this (i.e. specific amino acids), why the curves are right shifted with decreasing pH, and why this is logical in delivery of 02 to areas of higher demand. 100 Myoglobin 80- pH 7.6 60 pH 7.4 pll 7.2 40- pH 7.0 pH 6.8 20- Venous 0- 0. 20 10 60 80 Percent saturationWhat is the effect of pH on the binding of oxygen to hemoglobin (the Bohr Effect)? What happens to the percent saturation as a function of pO2 graph as a result of pH change (include graph)? Why is there a pH difference in tissues versus the lungs? Briefly describe how the Bohr Effect contributes to oxygen transport to the tissues.
- Calculate the pH of a blood plasma sample with a total CO₂ concentration of 25.7 mM and bicarbonate concentration of 24.4 mM. The relevant pK, of carbonic acid is 6.1. Enter the answer with three significant figures. pH =This graph shows the O2 binding curves of Hemoglobin. Which one is the R-state curve, and which one is the T-state? Why these curves are different comparing to the normal curve (middle one) 1.0 0.8 Observed hemoglobin- binding curve 0.6 0.4 0.2 0.0 50 100 150 200 p02 (torr) Y (fractional 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]