3. a. The figure below shows a llama, a relative of the camel. One amino acid in camel haemoglobin ß subunits has been replaced by a different amino acid in llama haemoglobin ß subunits. Llamas live at high altitudes and camels live at low altitudes. At high altitudes the partial pressure of oxygen is low. The figure shows dissociation curves for llama haemoglobin and camel haemoglobin. 100 llama 80 camel saturation of 60- haemoglobin with oxygen (%) 40 20 4 6. 8 10 12 14 16 partial pressure of oxygen (kPa) (i) What is the partial pressure of oxygen that results in a saturation of 50% in llama and camel haemoglobin? (ii) Explain why it is important for the survival of the llama that the llama haemoglobin dissociation curve is to the left of the camel haemoglobin dissociation curve. b. Complete the table regarding the affinity of oxygen in myoglobin and haemoglobin. In the blank, write “increase the affinity", “decrease the affinity" or “no change in affinity". Myoglobin Haemoglobin A decrease in the partial pressure of CO2 in the lungs An increase in the BPG level

3. a. The figure below shows a llama, a relative of the camel. One amino acid in camel haemoglobin ß subunits has been replaced by a different amino acid in llama haemoglobin ß subunits. Llamas live at high altitudes and camels live at low altitudes. At high altitudes the partial pressure of oxygen is low. The figure shows dissociation curves for llama haemoglobin and camel haemoglobin. 100 llama 80 camel saturation of 60- haemoglobin with oxygen (%) 40 20 4 6. 8 10 12 14 16 partial pressure of oxygen (kPa) (i) What is the partial pressure of oxygen that results in a saturation of 50% in llama and camel haemoglobin? (ii) Explain why it is important for the survival of the llama that the llama haemoglobin dissociation curve is to the left of the camel haemoglobin dissociation curve. b. Complete the table regarding the affinity of oxygen in myoglobin and haemoglobin. In the blank, write “increase the affinity", “decrease the affinity" or “no change in affinity". Myoglobin Haemoglobin A decrease in the partial pressure of CO2 in the lungs An increase in the BPG level

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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19. Which statement best describes at the molecular level why AB is the universal acceptor? a. It is the least common blood type. b. It contains both the type A and type B monosaccharides in addition to the core trisaccharide. only contains the core trisaccharide and does not have any additional sugars on it. d. Red blood cells of this type do not have any oligosaccharide markers. e. Type AB has a completely different oligosaccharide marker than A, B, c. and O.
3. The image below depicts 2,3-bisphosphoglycerate depicted in dark gray, and ß subunits are depicted in light gray. (BPG) bound to hemoglobin. The a subunits are BPG (a) Briefly explain how BPG regulates oxygen transport by hemoglobin and describe the critical chemical properties of BPG and its binding pocket.
#3 The heme group is a prosthetic group in: 80 F3 וח E D A) Fetal hemoglobin B) Adult hemoglobin C C) Myoglobin D) a and b E) a, b, and c F) b and c $ 4 F4 R F % 5 V ܀ F5 T G ^ B MacBook Air F6 Y H & ◄◄ F7 U N * 00 8 J DII F8 - M ( 9 K DD F9 O V I :) 0 4 F10 P |
2. It is known hemoglobinopathies, whi ch arise due to mutations in one of histidines a- or B- chains binding with the iron in the heme gro up.These mutations stabilize the iron in Fes form. Some drugs (eg. sulfonamides) or chemicals( eg.anilin) also can cause methemoglobinemia. Suggest, how change the properties of Hb in these cas es. For this:1)Describe the structure and function of Hb A as a transport protein. 2) Explain the role ofiron ions in act ive centers of Hb for the binding of O23) How many molecules of Oz can bind mutant Hb, if mutation occurs in a- subunits? 4) Why can ascorbic acid be used to tr eat of such patients.
. The mutation in hemoglobin at B82 Lys → Asp results in lowered O2-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site. A rationale for the observed reduction in O2-binding affinity is: A. The positive charge on the Asp side chain can form salt bridges with other negative charged side chains stabilizing R-conformer. B. The negative charge on the Asp side chain can form salt bridges with other positive charged side chains stabilizing the T-conformer. C. The Asp side chain mimics the positive charge on BPG. D. The Asp side chain mimics the negative charge on BPG. E. The Asp side chain is a nucleophile that attacks the BPG. F. BPG attacks the Asp side chain. G. Stabilization of the R-conformer favors O, release. H. Stabilization of the T-conformer favors O, release.
The hemoglobin in mammalian blood is usually thought of simply as increasing the amount of O2 that can be carried by each litter of blood. Explain how the presence of hemoglobin in the blood also makes possible the rapid uptake of O2 by the blood as it flows through the lungs.