100 80 75 HbA 60 Black line shows normal O2 dissociation curve for HbA S 50 - A K 40 - В 20 - 3.5 10 13.3 Oxygen tension (kPa) 24: Using the curve as a guide, predict whether the oxygen binding curve is shifted to the left (A) or to the right (B) for HbS.
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- 1.1 ;) The diagram on the right compares the O2 binding prop- 1.0 erties or normal adult hemoglobin (HbA) to those of one dubbed Hb Great-Lakes characterized by the mutation Leu(B68)His. In the dia- gram Y = fraction of heme groups with bound O2, and pO2, the par- tial pressure of O2 above the solution, is measured in units of torr or mmHg. Hb Great Lakes %3D 0.8 Hb A 0.6 Draw the corresponding Hill plot, being careful to reproduce graph- ically the dissociation equilibrium constant for O2 binding (Ko2) for Y each hemoglobin and to show the difference in the extent of allo- stery or cooperativity of subunit interaction in each type of hemo- globin. 0.4 You need draw only the central, linear portion of the Hill plot. 0.2 F State what is the likely magnitude of the Hill constant (nH) for HbA from your reading and state what is the likely range of the magni- tude of the Hill coefficient for Hb Great Lakes. 0 10 20 30 40 50 60 pO2 (torr)Studies of oxygen transport in pregnant mammals have shown that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two γ and two β subunits (γ2β2), whereas maternal erythrocytes contain HbA (α2β2). (a) Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain. (b) What is the physiological significance of the different O2 affinities? (c) When all the BPG is carefully removed from samples of HbA and HbF, the measured O2-saturation curves (and consequently the O2 affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2-saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2 affinity of hemoglobin? How can the above information be used to explain the different O2 affinities of…From the figure of O2 binding to myoglobin and hemoglobin (ignore the linemarked as T) as described in lecture (shown below) answer the following questions. a) Estimate the P50 for myoglobin from the plot. Show how this estimation isdetermined from the binding curve above. ( The first ghraph) b)Using YO2 = PO2/P50 + PO2 , calculate the fraction of O2 bound for myoglobin at 1 torr. (2nd graph) c)Using the binding curve on the previous page, show how you can estimate whatfraction of hemoglobin is bound near tissues at a pO2 of 30 torr and provide this value. If the pH were lowered, will the amount of O2 bound to hemoglobin at 30 torr increaseor decrease? Explain why this is so based on how this changes hemoglobin structure. If 2,3-BPG were added to the solution, will the amount of O2 bound to hemoglobin at30 torr increase or decrease? Explain why this is so based on how this changes hemoglobinstructure.
- 2,3 BPG is an allosteric effector that decrease haemoglobin affinity for oxygen by stabilizing the T-state of deoxyhaemoglobin. This lead to the release of oxygen to cells and body tissues for use. H atom and CO2 are also allosteric effector and can do same. How?PTP1B Substrate kcat Km. kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEP YLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 + 0.22 0.53 + 0.02 34.7 + 0.25 52.7 + 0.7 0.066 + 0.001 ) The units for kcat/KM in the above are given according to standard scientific notation. On this (d) ( basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?PTP1B Substrate kcat Km kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEPYLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 ± 0.22 0.53 + 0.02 34.7 + 0.25 52.7 ± 0.7 0.066 + 0.001 (d) (. ) The units for kcat/KM in the above are given according to standard scientific notation. On this basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?
- Measurements of oxygen binding by whok human blood, at 37 °C, at pH 7.4, and in the presence of 40 mm Hg of CO, and normal physiological lkvels of 2,3-BPG (5 mmol/L of cells), give the following: Po, (mm Hg) % Saturation (=100 x Yo) 10.6 10 19.5 30 27.4 50 37.5 70 50.4 85 77.3 96 92.3 98 (a) From these data, construct a binding curve, and estimate the percent oxygen saturation of blood at (1) 100 mm Hg, the approximate partial pressure of O, in the lungs, and (2) 30 mm Hg, the approximate partial pressure of Oz in venous blood. (b) Under these conditions, what percentage of the oxygen bound in the lungs is delivered to the tissues? (c) Using the data in Figure 7.27, repeat the calculation of part (b) if the pH drops to 6.8 in capillaries but goes back to 7.4 as CO, is unloaded in the lungs.Fetal gamma-subunits cause... Question 29 options: Decreased 2,3-bisphosphoglycerate binding and therefore reduces oxygen binding Decreased 2,3-bisphosphoglycerate binding and therefore facilitates oxygen binding Decreased 2,3-bisphosphoglycerate binding and therefore facilitates oxygen release Increased 2,3-bisphosphoglycerate binding and therefore reduces oxygen binding Increased 2,3-bisphosphoglycerate binding and therefore facilitates oxygen bindingDetermin the respiratory exchange ratio of C18H36O2(s) + 26O2(g) → 18CO2(g) + 18H2O(l)
- At 100% HbO2 saturation, all possible O2 binding sites are (bound or free).1.12 At elevated altitudes, the body adapts to the reduced barometric pressure to extract sufficient oxy- gen to permit normal metabolic functions and do work. For example, at an altitude of 3,650 m (close to 12,000 feet above sea level) the barometric pressure drops to 485 mmHg. For an oxygen pressure drop in the lungs of 30 mmHg, determine the oxygen uptake rate for a respiration rate of 20 breaths per minute. Estimate the oxygen saturation in venous blood if the hematocrit rises to 0.60 and the partial pressure of oxygen blood is at a partial pressure equal to 98% of the alveolar level.What is the actual change in free energy at 37°C for the phosphoglycerate mutase reaction converting 3-PGA to 2-PGA in erythrocytes if after drinking a glass of orange juice the [3-PGA] = 8 mM and the [2-PGA] = 0.08 mM? The standard change in free energy for the reaction is +4.5 kJ/mol. +16.3 kJ/mol O-6.5 kJ/mol O-7.3 kJ/mol -16.3 kJ/mol +7.3 kJ/mol