Select all answers that apply Some primitive animals have a hemoglobin that consists of two identical subunits.What would be the effect of this on the hemoglobin?It would have the same cooperativity as myoglobin.It would exhibit less cooperativity than hemoglobin.It would deliver more oxygen to the tissues than hemoglobin.It would have a hyperbolic binding curve.It would be less sensitive to the allosteric effectors such as 2,3-bisphosphoglycerate (BPG).

The structure of hemoglobin, particularly the number and arrangement of its subunits, significantly…

Answered: Some primitive animals have a…

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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Which of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environments
Which of the following is true about the T (tense) -->R (relaxed) transition of hemoglobin? A. The T state of hemoglobin binds oxygen with a higher affinity than the R state. B. The binding of O2 to a subunit T state can cause the transition of other subunits to the R state. C. The T state has a narrower pocket between b subunits than does the R state. D. When hemoglobin undergoes the T--> R transition, the structures of the individual subunits change dramatically.
You are studying with a friend who is describing the Bohr effect. She tells you that in the lungs, hemoglobin binds oxygen and releases hydrogen ion; as a result, the pH increases. She goes on to say that in actively metabolizing muscle tissue, hemoglobin releases oxygen and binds hydrogen ion and, as a result, the pH decreases. Do you agree with her reasoning? Why or why not?
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.
Hemoglobin exhibits positive cooperativity. What is positive cooperativity? Explain how hemoglobin exhibits this property.
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?
Which of the following statements is INCORRECT about how the components of hemoglobin are recycled? a. Iron ions are either stored in a phagocytic cell or circulate in the blood, bound to transferrin (a plasma protein). b. Each heme is stripped of its iron and converted to bilirubin, then excreted in bile. c. The alpha and beta chains are released into the bloodstream for use by other cells. d. Hemoglobin can be recycled only if phagocytized by macrophages.
The number of high-affinity binding sites in the T form of hemoglobin is _______The number of low-affinity binding sites in the T form of hemoglobin is _______
Myoglobin ... A. has higher affinity for O2 than hemoglobin does. B. consists of four polypeptide chains, just as hemoglobin does. C. has a lower affinity for O2 than hemoglobin does. D. is found in the interstitial fluids, in contrast to hemoglobin that is found in red blood cells. E. can bind four O2 molecules at once.
Suppose a hypothetical "molecule X" binds to hemoglobin (at a different site than the O2 binding site) and stabilizes the T state. How would you identify this effector? a. Positive homotropic effector b. Negative homotropic effector c. Positive heterotropic effector d. Negative heterotropic effector
Will a mutation from Distal histidine to phenylalanine shift the binding curve of hemoglobin?Will it shift the curve to the left or right, shift to myoglobin or no longer bind to O2?
How does hemoglobin bind O2 cooperatively? A. The binding of one molecule of O2 to one subunit of hemoglobin enhances the assembly of other subunits to form a complete hemoglobin protein. B. The binding of one molecule of O2 to one hemoglobin protein enhances the binding of a molecule of O2 to a different hemoglobin protein. C. The binding of one molecule of O2 to one subunit of hemoglobin enhances the affinity of the same subunit for more molecules of O2. D. The binding of one molecule of O2 to one subunit of hemoglobin enhances the affinity of other subunits for O2.

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