The following plot (percent of O2 bound versus [02]) shows three possible curves (A, B, C). In thiscase, "B" represents the normal oxygen transport protein. Suppose the local concentration of H+increases. How might this be represented on the graph?Percent O₂ boundAOA shift from B to CB[0₂]OH+ concentration has no effect (remains curve B)OA shift from B to A

The association between the partial pressure of oxygen (PO2) and the percentage of hemoglobin…

Answered: The following plot (percent of O2 bound…

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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Using the Nernst equation, calculate the equilibrium potential for Ca2 and for C1 from the following sets of data: a. Given [ Ca2+ ]0=1mM,[ Ca2+ ]i=100nM, find Eca2+ b. Given [ Cl- ]0=110mM,[ Cl- ]i=100mM, find Ecl
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)
) 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.
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.
In one type of hemoglobin mutant the amino acid change generates a strong ionic interaction stabilizing the T state conformation, but only under conditions of lower pH, e.g., at pH 7.2 compared to pH 7.6. Explain what effect this mutation would have on the amount of O2 delivered to the tissue. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the R state in tissues.
ATP is synthesized from ADP, P, and a proton on the matrix side of the in- ner mitochondrial membrane. We will refer to the matrix side as the "inside" of the inner mitochondrial membrane (IMM). (a) H* transport from the outside of the IMM into the matrix drives this process. The pH inside the matrix is 8.2, and the outside is more acidic by 0.8 pH units. Assuming the IMM membrane potential is 168 mV (inside negative), calculate AG for the transport of 1 mol of H* across the IMM into the matrix at 37 °C: Houtside) Hinside) (b) Assume three mol H* must be translocated to synthesize one mol ATP by coupling of the following reactions: ADP + P, + Hinskde) ATP + H,O(ATP synthesis) 3Hinside)(proton transport) 3Houtside)
Given: Factor VIIa is a man-made protein analog to Factor VII, which is involved in coagulation. (Answer a, b, and c)a. Identify both a competitive and non-competitive inhibitor for Factor VIIa b. Draw a graph showing how both of these molecules will change the Velocity/[S] graph, and explain why this is the case. c. What would a graph look like if both inhibitors were added?
Acid phosphatases are an important group of enzymes that can be detected in human bloodserum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyzebiological phosphate esters as follows:R-O-P-O3-2 + H2O -----> R-OH + HO-P-O3-2Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver,and prostrate gland. The enzyme from the prostrate gland is clinically important because anincreased activity in the blood is frequently an indication of cancer of the prostrate gland.Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acidphosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostrate gland in humanblood serum?
Heart and muscle cells, where myoglobin resides, maintains an intracellular pO2 of about 2.5 torr. Calculate the fractional saturation (for human myoglobin) if a small change (1 torr) in oxygen partial pressure occurs in either direction (ie what happens at 1.5 torr, what happens at 3.5 torr?) and explain how a small change in oxygen pressure dramatically changes the myoglobin oxygen binding.
In active muscle cells, the pO₂ is about 10 torr at the cell surface and 1 torr at the mitochondria (the organelles where oxidative metabolism occurs). Calculate the percentage of bound oxygen transported to the mitochondria of muscle cells by myoglobin (KD = 2 torr). A new oxygen transport protein that exhibits cooperative binding has been isolated and is being studied in the lab. Calculate the Ko value if Y = 0.76 when pO₂2 = 18 torr (assume n = 2.5). How does this compare to the K₂ value for hemoglobin? Does this protein bind more or less tightly to oxygen compared to hemoglobin?
What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.
To study the chemical properties of the blood hemoglobin of a vertebrate, it might seem convenient to remove the hemoglobin from the red blood cells so that the hemoglobin is in simple aqueous solution. However, removing the hemoglobin from red blood cells often promptly alters its O2-binding characteristics. Why?

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