answer both parts a. How does [H*] affect the ability of hemoglobin to bind O2? [Select]b. What is the physiological significance of thi V ( Select ]This allows for more release of 02 where CO2 has built up.This allows for less release of 02 where CO2 has built up.This does not change the release of 02 where C02 has built up.

Hemoglobin contains iron, which allows it to pick up oxygen from the air we breathe and deliver it…

a. How does [H*] affect the ability of hemoglobin to bind O2? [Select] b. What is the physiological significance of thi [ Select ] This allows for more release of O2 where CO2 has built up. This allows for less release of 02 where CO2 has built up. This does not change the release of 02 where co2 has built up.

a. How does [H*] affect the ability of hemoglobin to bind O2? [Select] b. What is the physiological significance of thi [ Select ] This allows for more release of O2 where CO2 has built up. This allows for less release of 02 where CO2 has built up. This does not change the release of 02 where co2 has built up.

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 19QP: A person was found to have very low levels of functional beta globin mRNA and therefore very low...

See similar textbooks

Similar questions

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?
Recall from your BI110 class that metabolically active tissues produce CO2 as a by-product of cellular respiration. Those metabolically active tissues require the O2 that is brought by hemoglobin for the same process (cellular respiration). Explain why the effect of pH on hemoglobin’s affinity for oxygen is consistent with delivering it to actively metabolizing tissues. (Hint: think about what effect the presence of CO2 has on the tissues…)
Select the hemoglobin variant(s) that are described by each statement. (a) The variant least likely to cause pathological symptoms. (b) The variant(s) likely to show pl values different from that of HbA on an isoelectric focusing gel. (c) The variant most likely to show a decrease in BPG binding and an increase in the overall affinity of the hemoglobin for oxygen. Answer Bank Hb Milwaukee Hb Cowtown Hb Memphis Hb Philly Hb Providence Hb Bibba HbS
Below is a fractional saturation curve for O₂ binding to adult hemoglobin. Assume that curve Y represents a condition at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve X represents a condition that Fractional saturation (0) 0.2 0.0 0 Tissue PO, (kPa) 12 Lungs
which of adult haemoglobin or foetal haemoglobin will have a lower P50 value for binding O2. Be sure to define the term P50 and mention at a molecular level what interactions and structure differences are contribute to the observed values.
Which of the following is incorrect about 2,3-bisphosphoglycerate (BPG)? It is highly (-) charged b. It prevents binding of O₂ to hemoglobin Oc. It binds only to the relaxed (oxy) conformation of hemoglobin Od. It binds in the space between the four subunits of hemoglobin a.
What Is the Effect of PO2 on Hemoglobin Saturation?
(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…
This graph shows the O2 binding curves of Hemoglobin. Which one is the R-state curve, and which one is the T-state? Why these curves are different comparing to the normal curve (middle one) 1.0 0.8 Observed hemoglobin- binding curve 0.6 0.4 0.2 0.0 50 100 150 200 p02 (torr) Y (fractional saturation)
Below is the O₂ binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). Fraction of Hb bound with Oxygen 1.0 0.8 0.6 0.4 0.2 0.0 0 20 40 pO2 (torr) 60 80 ABC c. Which curve lacks cooperativity? [Select] Hb 100 a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no other small allosteric molecules associated)? [Select] b. Which curve has the lowest affinity (as measured by the p50)? [Select]
(b) The diagram on the right illustrates the change in the p50 (partial pressure of O2 required to achieve 50% saturation) of hemoglobin and the 2,3-bis-phosphoglycerate (BPG) concentration in the erythrocytes of a person who spent 6 days hik- ing in the Andes Mountains of Peru. As the hiker climbs to higher and higher altitudes, the atmos- pheric pressure, including the partial pressure of O2, decreases. Yet the p50 increases, making it less favorable to achieve saturation of the hemo- globin. Explain. Pso (torr) Sea level 34 33- 32 31 30- 29 28 27 26 4530 m above- sea level (c) If individuals with the following mutant hemo- globins accompanied the hiker, evaluate the degree of respiratory distress that they would experience despite the increased erythrocyte BPG concentration. (In the ta- ble of mutants on the right, the mutation His(143)Asp, for instance, means that the His residue that occurs at se- quence position 143 on the ß-chain has been substituted by Asp.) Describe the…
Hemoglobin poz in lungs tissues (4,500 m) po2 in lungs (sea level) po2 in 8. Lack of 2,3-BPG can be deadly. 1.0 BPG = 0 mM 38% A) What is 2,3-BPG? How is it produced and why does hemoglobin need 2,3- 30% ВPG? 37%- Y 0.5 B) Under what physiological conditions are blood levels of 2,3-BPG elevated? C) How does an increased level of 2,3-BPG help our bodies compensate through crises of a low availability of external oxygen? Highlight the action of 2,3-BPG on hemoglobin in your answer. BPG - 5 mM at sea level BPG 8 mM at high altitudes (4,500 m) 4 8 12 16 pO2 (kPa) Figure 5-17 Lehninger Principles of Biochemistry, Seventh Edition O 2017 W. H. Freeman and Company