The graph below shows the O₂-binding curves for myoglobin (Mb) and hemoglobin(Hb).a.10080604020002040 60 80 100pO₂ (torr)a. Use the graph to determine the Kd of myoglobin for O₂ (show your approach).Write that in the provided space.b. What is the difference between myoglobin and hemoglobin that cause the O₂-binding curves to so be different? Answer in the provided space.c. Why is it important that hemoglobin has these particular O₂-bindingcharacteristics? Answer in the provided space.YO₂

Introduction: Oxygen binding is the binding of an oxygen molecule to a specific functional protein…

Answered: The graph below shows the O₂-binding…

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 following graph shows partial saturation (Y) of myoglobin (Mb), adult hemoglobin (HbA) and fetal hemoglobin (HbF) as a function of partial oxygen pressure (in mmHg). Use it to answer the question: Fetal hemoglobin ( biological function: HbF) demonstrates lower p50 than adult hemoglobin (HbA). This adaptation has the following A. Allow fetal hemoglobin form pentamer subunits. B. HbF has lower affinity for for O2 compared to adult Hb C. Allow fetal hemoglobin to effectively intercept oxygen from mother's hemoglobin. D. Allow fetal hemoglobin to replace myoglobin in muscles
After spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the concentration of 2,3- bisphosphoglycerate (2,3-BPG) in red blood cells increases. What effect would an increased concentration of 2,3-BPG have on the oxygen-binding curve for hemoglobin? Why would this adaptation be beneficial for functioning well at high altitude?
You want to measure the blood oxygen level in a drop of blood using a pulse oximetry device. If you have a light source at 700nm, and 1mm of path length. What must be the concentration of, a.Oxidized hemoglobin (HbO2) concentration in blood so that the light intensity at the output decreases to the one tenth of input intensity? b. Reduced hemoglobin (Hb) concentration in blood so that the light intensity at the output decreases to the one tenth of input intensity? c.At the concentration you found in b, what is Ii / If for oxidized hemoglobin?
Considering the quantity of hemoglobin in an erythrocyte and the oxygen-binding properties of hemoglobin, calculate how many molecules of oxygen one erythrocyte could carry?
In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.
People suffering with sickle cell anemia have a structural defect in hemoglobin (HB). The major reason for this structural change is mutation of glutamic acid to valine. This leads to a Exposure of polar amino acids, leading to disintegration of hemoglobin. b Burying of polar amino acids, leading to disintegration of hemoglobin. c Exposure of non-polar amino acids leading to long fiber formation. d Burying of non-polar amino acids thereby increasing hydrophobic interactions and formation of long fibres.
a) How much more O2 can be transported by the blood when erythrocytesleave the lungs? Consider that a normal adult has a concentration of 15 g hemoglobin/100 mL of bloodand that the hemoglobin is 98% saturated with O2 at the usual pO2 of 100 torr in the lung at sea level. b) On the basis of the graph, explain how myoglobin facilitates the diffusion of O2 through muscle cells. Would myoglobin be effective as an O2-transport protein in cells of other tissues? Explain.
What is the biological advantage to the sigmoidal binding curve of hemoglobin for oxygen? A. It ensures that hemoglobin has a high affinity for oxygen. B. It allows hemoglobin to bind oxygen irreversibly. C. It ensures that hemoglobin can bind oxygen only weakly. D. It allows hemoglobin to shift between low and high affinities for oxygen.
a.What is the difference between the 5th and 6 coordination sites in the heme group? b.What is the change of the oxygen dissociation curve represented by hemoglobin before and after dissociation into subunits? Briefly explain why.
The concentrations of lactate in blood plasma before, during, and after a 400 m sprint are shown in the graph.(a) What causes the rapid rise in lactate concentration?(b) What causes the decline in lactate concentration after completion of the sprint? Why does the decline occur more slowly than the increase?(c) Why is the concentration of lactate not zero during the resting state?
The equation describing the linear relationship between hemoglobin concentration and absorbance at 520 nm is y=0.0523x+0.011. If the absorbance value is 0.6, calculate the % hemoglobin in whole blood.
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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