Please asap (a) The variant least likely to cause pathological symptoms.Hb Memphis(b) The variant(s) likely to show pl values different from that of HbA on an isoelectricfocusing gel.HbS Hb Cowtown Hb Memphis Hb Bibba Hb MilwaukeeHb PhillyHb Providence(c) The variant most likely to show a decrease in BPG binding and an increase inthe overall affinity of the hemoglobin for oxygen.Hb MilwaukeeAnswer BankHb MilwaukeeHb ProvidenceHb BibbaHb CowtownHb MemphisHb PhillyHbS

Hemoglobin is a protein molecule found in red blood cells which transports oxygen (O2) from the…

Answered: (a) The variant least likely to cause…

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 3SQE

See similar textbooks

Similar questions

A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?
What is oxyhemoglobin? Where does it form?
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.
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
Sketch out the binding site of Hemoglobin with oxygen bound . ( You can abstract the Heme ring out i.e. not draw each chemical bond). Please label both imported HIS residues.
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 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
d) Determine which statements apply to hemoglobin, myoglobin, or neither (you can write in the corresponding numbers for each statement, as appropriate) Hemoglobin Myoglobin Neither 1. Oxygen binds irreversibly to this molecule.2. This molecule has greater affinity for oxygen.3. The oxygen dissociation curve is sigmoidal in shape.4. Carbon monoxide binds at an allosteric site, lowering oxygen binding affinity.5. The binding pattern for this molecule is considered cooperative.6. This molecule delivers oxygen more efficiently to tissues.7. As oxygen binds to this molecule, the shape of the molecule changes, enhancing further oxygen binding.8. The oxygen dissociation curve is hyperbolic in shape.
A The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding oxygen to hemoglobin would be altered by the change in conditions noted. 2. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 poz pO2
Q) Following an intensive course of chemotherapy, a 48-year-old woman had a thorough laboratory evaluation, selected results of which are: Hemoglobin 8 g/dL, hematocrit 32% Arterial blood gases: pH 7.38, Pa.CO₂ 42 mm Hg, bicarbonate 25 mEq/L, Pa.O2 62 mm Hg, O₂ saturation 92%. Given that the O2 binding capacity of hemoglobin is 1.34 ml/g, calculate the O2 capacity of her hemoglobin. A) 9.86 ml/dL B) 9.86 mm Hg C) 9.86 mEq/L D) 10.72 ml/dL E) 10.72 mEq/L Ans: D 6.11. Following an intensive course of chemotherapy, a 48-year-old woman had a thorough laboratory evaluation, selected results of which are: Hemoglobin 8 g/dL, hematocrit 32% Arterial blood gases: pH 7.38, Pa.CO₂ 42 mm Hg, bicarbonate 25 mEq/L, Pa.O₂ 64 mm Hg, O₂ saturation 92%. Given that the O2 binding capacity of hemoglobin is 1.34 ml/g, calculate the O2 content of her arterial hemoglobin. A) 9.86 ml/dL B) 9.86 mm Hg C) 9.86 mEq/L D) 10.72 ml/dL E) 10.72 mEq/L Ans: A
Blood in our body changes color as a function of its oxygenation state. Given the spectral data below, calculate the absorbance of red light (600 nm) of fully oxygenated and deoxygenated blood. Using this data, determine what percentage of red light would go through a sample of blood that is 50% oxygenated. Assume the patient has a hemoglobin concentration of 10 mM and pathlength of 1 cm.
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)

SEE MORE QUESTIONS

Recommended textbooks for you

Human Physiology: From Cells to Systems (MindTap …

Biology

ISBN:

9781285866932

Author:

Lauralee Sherwood

Publisher:

Cengage Learning

Human Heredity: Principles and Issues (MindTap Co…

Biology

ISBN:

9781305251052

Author:

Michael Cummings

Publisher:

Cengage Learning

Human Biology (MindTap Course List)

Biology

ISBN:

9781305112100

Author:

Cecie Starr, Beverly McMillan

Publisher:

Cengage Learning

Human Physiology: From Cells to Systems (MindTap …

Biology

ISBN:

9781285866932

Author:

Lauralee Sherwood

Publisher:

Cengage Learning

Human Heredity: Principles and Issues (MindTap Co…

Biology

ISBN:

9781305251052

Author:

Michael Cummings

Publisher:

Cengage Learning

Human Biology (MindTap Course List)

Biology

ISBN:

9781305112100

Author:

Cecie Starr, Beverly McMillan

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS