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- 5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 a DCM 23 Tor • DCM 50 Torr x DCM 100 Torr Symbols: o, 0 Torr DCM; O, 23 Torr DCM A, 50 Torr DCM x, 100 Torr DCM. 80 40 (1 Torr = 1 mm Hg.) The solutions buffered to pH 7.4. 20 were 0.5 1.0 1.5 2.0 log po2 % OXYGENATION5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 a Dсм 23 Torr Symbols: в Dсм 50 Torr x DCM I00 Torr o, 0 Torr DCM; O, 23 Torr DCM A, 50 Torr DCM x, 100 Torr DCM. 80 60 40 (1 Torr = 1 mm Hg.) 20 The solutions were buffered to pH 7.4. 0.5 1.0 1.5 2.0 log p02 (a) (* Hill plots. Label the axes and indicate on both the plot above and the Hill plot where the value of the dissociation equilibrium constant Ka for O2 binding is defined for 0 and 100 Torr of dichloromethane For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of Kd Hb(O2)n Hb + nO2 % OXYGENATION1.1 ;) 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)
- Carbon monoxide binds the heme of hemoglobin in the same position as O2; however, it binnds 200 times better than 02 If we use a value of 40 torr for hemoglobin's Pso for 0z. what is its P5o for CO? 0.05 torr 0.20 torr 5 torr 200 torr O 8,000 torrA patient presents to the emergency department in a critical condition. The patient’s blood was tested and the concentration of carbonic acid (H2CO3) was found to be 4.0×10-4 M and bicarbonate ion (HCO3-) 3.062×10-3 M. Ka = 4.3 × 10-7 H2CO3(aq) ⇌ HCO3-(aq) + H+(aq) Show all calculations including equation(s) used. Calculate the pH of the patients’ blood. Based on your answer would you say the patient is suffering from Acidosis or Alkalosis?Phenylephrine and nafazolin solutions are used as decongestants to relieve nasal congestion. Your patient has been given the following prescription below. You need to prepare 100 g of this nasal spray and make it isotonic. 1. There is an available 25% w/w Phenylephrine solution in the pharmacy. How many g of this solution will you need to supply the needed 0.5% of the patient? A. 1.0 g В. 1.5 g С. 2.0 g D. 4.0 g 2. Given the amount calculated on the previous item, and if the E value of phenylephrine HCl is 0.32, calculate its corresponding sodium chloride tonicic equivalent. А. 0.16 B. 0.64 С. 1.60 D. 6.40 3. If the E value of nafazolin is 0.27, what is the sodium chloride tonicic equivalent of the patient's needed nafazolin? A. 0.0135 B. 0.1350 1.3500 D. 13.500 4. What is the combined sodium chloride tonicic equivalent of the remaining ingredients (edetate disodium (E =0.24) and sodium metabisulfite (E = 0.7)? A. 1.060 B. 0.106 С. 1.290 D. 0.129 5. To make the solution isotonic, what…
- Determine the concentration of [Ser] at 75s at T=335K time (s) [Ser] at T=335 0.150 5 0.143 20 0.120 40 0.090 90 0.015 0.005 0.047 M 0.038 М 0.088 МWhich of the following is correct concerning the oxygenation plot of proteins X and Y shown below? Y (fraction saturation) 1.0 0.8 0.6 등 0.4 0.2 0.0 0 20 Oxygen binding plot 40 flog ha 60 p02 (torr) 80 100 X YThe order is for Ceftin 0.25 gPO, bid. On hand you have Ceftin 125mg tablets. How many tablets should you give?
- 2. j The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding of oxygen to hemoglobin would be altered by the change in conditions noted. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 po2 pO2The figure shows three oxygen binding curves for hemoglobin in the red blood cells of normal blood, pH 7.6. The middle-dashed line is the standard line for human hemoglobin. Lines A and B represent two experimental conditions your lab partner plotted but forgot to label. 1 0.8 0.6 0.4 0.2 | pO2 Q. which one is the hemoglobin you reduced the concentration of 2,3- bisphosphoglycerate in? and which line is the data from the hemoglobin you changed the pH to 7.3?Paclitaxel is used to treat ovarian cancer by infusion at a concentration of 0.6 mg/mL over 24 hours. A dose of 135 mg/m² has been prescribed for Sero. Sero is 1.06 m tall and weighs 92 kg. Paclitaxel comes in vials of 150 mg/25 mL. Calculate the volume of 5%w/v glucose solution that would be required to dilute the concentrated solution to prepare an paclitaxel solution of the required strength.