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 60 p02 (torr) 40 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 - myoglobin
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- Below is the O2 binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). A Hb 20 40 60 80 100 pO2 (torr) 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 p5o)? [ Select ] c. Which curve lacks cooperativity? [ Select ] Fraction of Hb bound with Oxygen 0.2 0.4 0.6 0.8 0'0 >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.Hemoglobin poz in lungs tissues (4,500 m) po2 in lungs (sea level) po2 in 8. Lack of 2,3-BPG can be deadly. 1.0 BPG = 0 mM 38% A) What is 2,3-BPG? How is it produced and why does hemoglobin need 2,3- 30% ВPG? 37%- Y 0.5 B) Under what physiological conditions are blood levels of 2,3-BPG elevated? C) How does an increased level of 2,3-BPG help our bodies compensate through crises of a low availability of external oxygen? Highlight the action of 2,3-BPG on hemoglobin in your answer. BPG - 5 mM at sea level BPG 8 mM at high altitudes (4,500 m) 4 8 12 16 pO2 (kPa) Figure 5-17 Lehninger Principles of Biochemistry, Seventh Edition O 2017 W. H. Freeman and Company
- Discuss the metabolic changes that take place in aspirin. How can it cause methemoglobenemia?Select the hemoglobin variant(s) that are described by each statement. (a) The variant least likely to cause pathological symptoms. (b) The variant(s) likely to show pl values different from that of HbA on an isoelectric focusing gel. (c) The variant most likely to show a decrease in BPG binding and an increase in the overall affinity of the hemoglobin for oxygen. Answer Bank Hb Milwaukee Hb Cowtown Hb Memphis Hb Philly Hb Providence Hb Bibba HbSThe FIGURE 1 below shows the Bohr shift occurs in fetal haemoglobin (P and Q) and for maternal haemoglobin (R and S). 100 90 80 P pH 7.6, Q pH 7.4 70 60 R pH 7.6 -S pH 7.4 50 40 30 20 10 20 40 60 80 100 120 Po,(mm Hg) FIGURE 1 a) Define Bohr shift. State the effect of Bohr shift on the oxygen dissociation curve. b) Compare the oxygen dissociation curve for fetal and maternal haemoglobin. Explain. c) What happens to the oxygen dissociation curves when the pH is lowered? Explain. d) Give TWO reasons why an expectant mother is advised to give up the smoking. e) Sketch the curve for fetal myoglobin at pH 7.6. Label the curve as X. Percent O2 saturation of hemoglobin
- Based on the image below, select the correct statement. Complex II QH₂ Q- 10 2 HO 2 HO Fe-S (2.8 FADH₂ FAD- Succinate Fumarate https://canvas.uts.edu.au/assessment questions/356986/files/1562694/download? 2e verifier-eUTT3hYal2YYTWlywV8TIFA3USmzCsM52jECmvTo O Succinate is reduced to fumarate O Succinate is oxidised to FAD O The Fe-S center shuffles electrons from FAD to ubiquinone (Q) O The Fe-S center shuffles electrons from FADH2 to ubiquinone (Q) The Fe-S center shuffles electrons from FADH2 to ubiquinonol (QH2) W 88 16°CA child weighing 22 lbs, has an infection and the doctor orders erythromycin drops 2.0 mLp.o. q6h. The bottle states that the usual dosage is 20.0-40.0 mg/kg/day, and there are35.0 mg per 1.5 mL. Find the min and max dosage per day in mL. Is the order within therecommended dosage?All of the following conditions would result in an increase in these cells (blue arrow) EXCEPT 1. hemorrhagic anemia 2. pernicious anemia 3. iron-deficiency anemia 4. hemolytic anemia 5. high altitude living 6. polycythemia vera Choose from the following: (A) 2 and 3 (B) 1 and 4 (C) 5 and 6 (D) 2 and 5 (E) 1 and 2
- Red Cell Index Iron Deficiency Anemia (microcytic hypochromic) Macrocytic Anemia (normochromic) Anemia of Chronic Disease (normocytic normochromic) MCV Low High Normal MCHC Low Normal Normal MCH Low High Normal Compare the hematocrits, haemoglobin contents, red blood cell counts, MCV, MCHC and MCH of sample X and Y with standard values. Give comments on the two samples base on the red cell indices (Which subject may be more suspected to suffer from anemia?) Normal Range of MCV: 80-98 femtoliters, fL Normal range of MCHC: 320-360 g/L Normal range of MCH: 27-32 picograms, pg Samples X Y MCV (femtoliters, fl) = 84.73 fL = 69.53 fL MCHC (g/L) = 258.87 g/L =370.52 g/L MCH (pictograms, pg) = 21.93 pg = 25.76 pgMae Raven has iron deficiency anemia. She complied to eat foods high in iron such as green leafy vegetables and red meat in adequate amounts. She also takes in Vitamin C supplements. She drinks iron fortified milk twice a day. Three weeks after, a returned check-up was made, still the hemoglobin is at low level. a.) Discuss the cause of persistently low hemoglobin levels, in relation to Food-food and Food-drug interactions.Why is Hgb 8.3 L is abnormal for Myocardiac infarction patient?