7L.4.2 Hemoglobin is the oxygen carrier in the blood of most vertebrates.3 bound O2,PO₂-100 mm Hgmost likely to bind oxygen moleculesHow is hemoglobin's affinity for oxygen affected by the presence or absence of oxygen?Rank hemoglobin molecules with the described conditions from most likely to bind oxygen molecules to most likely to release oxygen molecules. (For help approaching this problem, open Hint1.)► View Available Hint(s)1 bound O2,Po₂ = 100 mm Hgß chains$$Ea chainshemoglobin3 bound O2,PO₂ = 40 mm HgFrom Biology by Campbell and ReeceⒸ 2008 Pearson Education, Inc.ironheme1 bound O2,PO₂=40 mm HgResetHelpmost likely to release oxygen molecules

A protein that binds a ligand with high affinity in high concentration environment is unlikely to…

Answered: Hemoglobin is the oxygen carrier in the…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter46: Gas Exchange: The Respiratory System

Section: Chapter Questions

Problem 9TYK

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(b) The diagram on the right compares O2-dissoci- ation curves for human hemoglobins characterized by dif- ferent p50 values. If Ko2 represents the equilibrium disso- ciation constant for oxygen binding, e.g., Hb(02)n Hb + nO₂ show the relationship between Ko2 and p50. Assign one of the curves (a, b, e) that best approxi- mates the Ko2 of each of the mutant hemoglobins in the table above including HbA where Ko2 represents the equi- librium dissociation constant for oxygen binding. If no curve is present for any of the mutant hemogobins, state the rea- son why the mutant is not represented. Indicate on the graph where its p50 would lie. PERCENT SATURATION 100- 80- 60- 40- 20- PARTIAL PRESSURE OF OXYGEN lungs veins muscle 0- 0 20 bc/d T 100 120 140 40 60 80 OXYGEN PRESSURE (millimeters of mercury) (c) Of the mutant hemoglobins in the table above, which form a hydrogen bond stabilizing the R (oxy) conformation similarly to that in wild type HbA. Justify this statement on the basis of the…
1. The diagram on the right compares the O2 binding prop- 1.0 r erties of 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 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 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)
Below are multiple oxygen binding affinity curves for hemoglobin. The affinity curve for normal hemoglobin in blood is represented by curve "D," at a pH of 7.2 and at a concentration of 5mM BPG and 26 mM CO2. O₂ saturation (%) 100 Answer 1: B Answer 2: [Select] Answer 3: B Answer 4: 80 A 60 1. How would changes to acidity, BPG concentration and CO₂ levels affect the binding affinity curve and p50? lower than Answer 5: E 40 1. BPG concentration is decreased to 3mM: The binding affinity curve would look like B. The p50 would be lower than normal (D). 2. pH is increased to 7.6: The binding affinity curve would look like B. The p50 would be [Select] normal (D). 20 3. CO₂ concentration is increased to 30 mM: The binding affinity curve would look like. [Select] The p50 would be Answer 6: 0 normal (D). II. The hemoglobin has been treated with a denaturing solution which disrupts quaternary structure only, and has a binding affinity resembling myoglobin. The binding affinity curve would look…
Below is the oxygen saturation curve for myoglobin and hemoglobin at a pH of 7. The p50 for myoglobin is indicated by the dashed lines on the graph. Mb and Hb O2 saturation: pH 7 10 0.8 Myoglobin 0.6 P50 = 0.2 0.4 Hemoglobin 0.2 - 0.0 pO2 [kPa] Which of these molecules (Mb/Hb/neither or both) has cooperativity? [ Select ] What would you expect to happen to the p50 of myoglobin if the pH were decreased to a pH of 4? [ Select ] Fraction saturation
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 a structural variant of hemoglobin, HbF, consisting of two a and two y (a2 y2), whereas maternal erythrocytes contains HbA (a2 B2). 1.0 HbF +BPG e 0.5 HbA +ВPG 2 4 6 8 10 pO2 (kPa) What is the physiological significance of the different O2 affinities?
From your graph, estimate the P50 for normal hemoglobin and the mutant corresponding to your student number and explain if these results support your expectations regarding the mutant's oxygen affinity compared to normal hemoglobin. ف C Normal Yakima pO2 (torr) Yo2 Yo2 10 0.05 0.10 15 0.10 0.25 20 0.25 0.45 25 0.50 0.70 30 0.75 0.85 40 0.85 0.95 60 0.95 0.98 H
Figure 5 shows oxyhemoglobin dissociatlon curves at pH 7.2 and pH 7.4. Which of the following is true at PO2 less than 40 mm Hg? 27. % saturation af haemogiobin 100 pH 7.4 80 60 pH 7.2 40 + 20 10 20 30 40 50 60 70 Po; (mm Hg) Figure 5 A. Hemoglobin retains less O2 at pH 7.4 compared to pH 7.2. B. Hemoglobin retains less O2 at pH 7.2 compared to pH 7.4. C. The release of O2 from hemoglobin is not influenced by the production of CO2. D. At pH 7.2 where CO2 production is less than pH 7.4, hemoglobin releases less O2.
pO2 in tissues p02 in lungs 1.00 Oxygen-binding curves for normal Normal Hb hemoglobin, 50% carboxyhemoglobin, and hemoglobin from 0.8 an anemic individual. 0.6 Y 50% COHB 0.4- Anemic individual 0.2 4 8 12 pO2 (kPa) Box 5-1 Figure 2 Lehninger Principles of Biochemistry, Seventh Edition O 2017 W. H. Freeman and Company r aye i UIE I. Answer the following questions. Do not forget the units. 1) From the binding curve for normal Hb shown above, what is the Ka of normal hemoglobin?
o Suppose Gina climbs a high mountain where the oxygen partial pressure in the air decreases to 70 torr. Assume that the pH of her tissues and lungs is 7.4 and the oxygen concentration in her tissues is 20 torr. The P50 of hemoglobin is 26 torr. The degree of cooperativity of hemoglobin (n) is 2.8. Estimate the percentage of the oxygen-carrying capacity that she utilizes. oxygen-carrying capacity utilized: After Gina spends a day at the mountaintop, where the oxygen partial pressure is 70 torr, the concentration of 2,3-bisphosphoglycerate (2,3-BPG) in her red blood cells increases. Why does increasing the concentration of 2,3-BPG in Gina's blood cells help her function well at high altitudes? The P50 value of her hemoglobin increases, promoting oxygen delivery to tissues. The P50 value of her hemoglobin decreases, causing more blood-to-tissue oxygen offloading. The extra 2,3-BPG stabilizes the relaxed, or R, state of hemoglobin, increasing oxygen binding. Excess 2,3-BPG binds oxygen…
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 a structural variant of hemoglobin, HbF, consisting of two a and two y (a2 y2), whereas maternal erythrocytes contains HbA (a2 B2). 1.0 ·HbF +BPG 0.5 HbA +ВPG 2 4 6 8 10 pO2 (kPa) 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?
1. The diagram on the right compares the O₂ binding prop- erties of normal adult hemoglobin (HbA) to those of one dubbed Hb Great-Lakes characterized by the mutation Leu(368) 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. 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. You need draw only the central, linear portion of the Hill plot. 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. 1.0 0.8 0.6 0.4 0.2 Hb Great Lakes 0 10 20 Hb A 1 1 30 40 pO₂ (torr) I 50 60
Hemoglobin and myoglobin both use heme as their prosthetic group and they both bind O2. However, their O2-binding curves indicate these proteins have different activities. What lind of information can be learned about the differences between the curves?

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