giapis Below Show 02-binding curves of several proteins including myoglobin (Mb) and hemoglobin (Hb). If curve 3 (----) represents the 02 binding behavior of normal hemoglobin, which curve represents an 02-binding transporter with the same p5o as normal hemoglobin? 1.0- 2 3 4 5. YO2 0.5- 0.0 pO,(torr) O A. 1 В. 2 C. 4 D. 5 O E. Both "2" and "4"

giapis Below Show 02-binding curves of several proteins including myoglobin (Mb) and hemoglobin (Hb). If curve 3 (----) represents the 02 binding behavior of normal hemoglobin, which curve represents an 02-binding transporter with the same p5o as normal hemoglobin? 1.0- 2 3 4 5. YO2 0.5- 0.0 pO,(torr) O A. 1 В. 2 C. 4 D. 5 O E. Both "2" and "4"

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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Similar questions

Here is a chloride cell in the gill epithelium of a fish. For reference, NKA = Na+/K+ ATPaseNKCC = Na+/K+/Cl- cotransporter. Given that the chloride cells of salt water fish have the NKCC transporter on the basal (bottom) side of the epithelium, what do you predict regarding the NKCC transporter in chloride cells of freshwater fish? A. The transporter must move chloride in the opposite direction, also from the bottom side of the cell. B. The NKCC transporter, as localized in salt water fish, could also work in freshwater fish. C. The transporter must move chloride in the opposite direction, but from the apical (top) side of the cell. D. A transporter is not needed to move Cl- ions into cells from fresh water.
What qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.
One molecule of 2,3-bisphosphoglycerate (BPG) binds to one molecule of haemoglobin (Hb) in a central cavity of the haemoglobin molecule. Is the interaction between BPG and Hb stronger or weaker than it would be if BPG were bound to the surface of the protein instead? Explain your answer.
Approximate P50 for myoglobin from its binding curve. Approximate P50 for normal hemoglobin and the hemoglobin mutant from the binding curve. At low pO2 (below 20 Torr), which binds O2 with greater affinity, normal hemoglobin or the hemoglobin mutant? At high pO2 (above 30 Torr), which binds O2 with greater affinity, normal hemoglobin or the hemoglobin mutant? Which protein, normal hemoglobin or the hemoglobin mutant, transports O2 more efficiently? Briefly explain your answer.
One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).
A mutation in the alpha globin gene that introduced one additional basic amino acid residue in the BPG binding pocket would: (select one) a) Eliminate Hb’s positive cooperativity. b) Decrease Hb’s O2 binding affinity. c) Increase Hb’s O2 binding affinity. d) Increase O2 binding in muscle and decrease it in lungs. e) Decrease O2 binding in muscle and increase it in lungs. f) It would have no effect on the adult form of Hb.
) Dr Merrick is so excited to know the affinity constant Kd values for O2 binding to mammoth OBP and elephant hemoglobin at pH=7, that he starts speculating about the kinetics of binding to O2. If the ka value of mammoth EHb-O2 complex was the same as the ka value of mammoth OBP-O2 complex, what would be the ratio between the kd values of these complexes? Explain your reasoning. Hint: we are looking for the ratio kd(EHb)/kd(OBP) at pH=7.
r^2=6Dt , where D is the diffusion coefficient of thediffusing object and t is the time that the object is allowed to diffuse. If the diffusion coefficient, D, of a small protein is 5 x 10^-10 m2 s-1, how long (on average) does ittake for the protein to diffuse across a parasitic wasp that is 189 um long ?
In an experiment, hemoglobin is dissociated in a buffer and a subunit is isolated to study for its oxygen binding affinity. (i) What is the shape of the oxygen dissociation curve is expected in the experiment?Explain why. (ii) Is the Km of the isolated subunit higher or lower than the Km of an intact hemoglobin?
A new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?
he doctor also mentioned a new treatment for Sickle Cell Disease to JJ called Voxelotor (Oxbryta). Voxelotor binds to the a-globin chain and alters the structure of HbS stabilizing it in the R-state (relaxed state). Q7: In the presence of Voxelotor would you expect the affinity of HbS for O2 to increase or decrease? Q8: How would you classify the mechanism of action for Voxelotor? Q9: Voxelotor's structure is shown below. What would you expect the overall charge of the molecule to be in the blood (pH = 7.4) Pyridinium pKa = 2.6 Phenol pKa = 8.3
Interpret the effect of hyperkalemia with reference to Goldman’s equation. a) What happens to rate of K+ diffusion at the MRP equilibrium with elevated extracellular [K+] (and unchanged intracellular [K+])?b) Since this diffusion rate determines the “permeability” of the cell to that K+ ion, what happens to PK+ as a result of this elevated extracellular K+? (Hint- it HAS changed.)c) Since PK+ has changed, and PNa+ is unchanged, what happens to the MRP as a result of this change in PK+? Explain with specific reference to Goldman’s equation but there is no need to cite or calculate any specific numbers, just generalize the result.