3) 3. What statement below is false?(a) 2,3-Bisphosphoglycerate (BPG) reducesbinding of O₂ to hemoglobin from almosthyperbolic to sigmoidal shape by stabilizingthe T state.O (b) CO₂ is an end product of cellularrespiration that is transported by Hb fromtissue to lungs in the form of a carbamatemoiety.(c) Four molecules of BPG bind to onemolecule of hemoglobin.O (d) Both H* and CO₂ bind in a mannerinversely related to the binding of 0₂(e) CO2 binds as a carbamate group to thea amino group at the amino terminal endof each Hb chain.

Hb is a protein responsible for carrying both O2 and CO2 in blood. 1 Hb protein is composed of 4…

Answered: (a) 2,3-Bisphosphoglycerate (BPG)…

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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The 2-3 phosphoglycerate (BFG) binds to the central gap formed by the hemoglobin monomers (a2b2) facilitating the reversible release of oxygen. Approximate relationships between BFG concentrations in red blood cells and Pos in hemoglobin are in the table.a) Draw the reaction schemeb) Write the forces that condition the union between hemoglobin and BFG
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)
A crocodile, which can remain underwater without breathing for up to 1 hour drowns its air-breathing prey, then dines at its leisure. An adaptation that aids the crocodile in doing so is that it can utilize virtually 100% of the O2 in its blood whereas humans, for example, can only extract about 65% of the O2 in their blood. Crocodile Hb does not bind BPG. However, crocodile deoxyHb preferentially binds HCO3-. How does this help the crocodile obtain its dinner? Please help explain why/if this is the answer, thank you! As CO2 concentrations increase so will the concentration of HCO3-. The HCO3- preferentially binds to the crocodile's deoxyhemoglobin, which allosterically prompts the hemoglobin to assume the deoxy conformation and thus release its O2.
Given the oxygen dissociation curves, which of the following statements are correct? Which residue in HbA β do you think contributes the most to the increased interaction between HbA aand 2,3‑BPG?
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.
Determin the respiratory exchange ratio of C18H36O2(s) + 26O2(g) → 18CO2(g) + 18H2O(l)
2.(a) The two diagrams on the right compare O2 binding pro- perties of Hb Kariya, a human hemo- globin characterized by the mutation Lys(a40)Glu, with those of HbA as a function of pH ranging from pH 9.0 to pH 6.95. One O2 saturation curve () illustrates the O2 binding proper- ties at pH 7.5 in the presence of 2 mM inositol hexaphosphate (IHP). (IHP is found in avian red blood cells. and binds more tightly than BPG be- cause of the additional negative charges.) log [Y/(1 - Y)] Hb Kariya + IHP (b) The diagram on the right illustrates sche- matically the interaction of the side chain of the aLys40 residue with the C-terminal -COOH group of the B-sub- unit in HbA. In Hb Kariya with a Lys(a40)Glu mutation, which allosteric conformation R or T is destabilized, and which allosteric HbA conformation is illustrated on the right? Explain log (P) Excluding the O2 saturation curve collected in the presence of inositol-hexaphosphate (IHP), indicate with an arrow for both hemoglobins the plot…
In nature, there are some organisms that are unable to perform aerobic respiration in the presence of oxygen. What could be the possible reason(s) behind this phenomenon? (Answe in 120 words, 5 reasons would be helpful) Thanks
3. (a) The (acid) Bohr effect is defined as the up- take of protons by hemoglobin molecules at pH ≤ 6.5 as O2 is dissociated from the protein in solution. Approxi- mately 0.6 mole protons are taken up for each mole of O2 released by normal human hemoglobin. The effect is seen as a "shift to the right" in the O2 dissociation curves with decrease in pH, indicating that the O2 binding affinity of Hb decreases at lower pH. On the right is a diagram compar- ing the pH dependence of the p50 values of Hb Deer Lodge [His(32)Arg] (filled symbols) and of HbA (- - -) in the absence of organic phosphates, i.e., “Stripped”, and in the presence of saturating concentrations of IHP. On the basis of the definition of the Bohr effect given above, explain why the data in the diagram reflect the Bohr effect for the two types of human hemoglobins. log p50 1.5 1.0 0.5 0.0 -0.5 5 6 stripped 7 pH +DPG 8 IHP 9 (b) The Bohr effect is generally decreased in Hb Deer Louge compared to that in HbA. Provide an…
One of the molecules listed below is effective in reducing O2 affinity of human Hb in the absence of BPG: (1) Glucose 6-phosphate (2) Inositol hexaphosphate (3) Maleic acid (4) Lactate (5) Arginine - Interestingly, this molecule plays the role of BPG in bird and turtle hemoglobin. A) Write the chemical structure of each molecule mentioned above. (B) Predict what molecule is most effective in preventing O2 binding to Hb. In 20 words or less explain the rationale for your prediction
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…
Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain astructural variant of hemoglobin, HbF, consisting of two α and two γ subunits (α2 γ2 ), 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 fetal and…

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