Answered: Under appropriate conditions,… | bartleby

Human Physiology: From Cells to Systems (MindTap Course List)

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

See similar textbooks

Related questions

Question

Please explain the answer thoroughly.

Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated
a subunits binds oxygen, but the O2-saturation curve is hyperbolic rather than sigmoidal.
In addition, the binding of oxygen to the isolated a subunit is not affected by the presence
of H*, CO2, or BPG (2,3-Bisphosphoglyceric acid). What do these observations indicate
about the source of the cooperativity in hemoglobin?

Expert Solution

Trending now

This is a popular solution!

Step by step

Solved in 2 steps

SEE SOLUTION Check out a sample Q&A here

Blurred answer

Similar questions

Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?
Increasing concentrations of either 2,3-bisphosphoglycerate (BPG) or protons (H +) cause a ____________ ( rightward OR leftward) shift of the hemoglobin/oxygen binding curve. However, the mechanisms by which these two substances mediate this effect are distinct. Compare & contrast the way by which BPG and protons interact with hemoglobin and thereby influence its structure and function
a) How does the fetal hemoglobin differ from the maternal hemoglobin in regards to structure and function? b) Explain the Bohr effect by drawing oxygen dissociation curves on a single graph that highlight changes in the hemoglobin affinity for O2 c) Describe the molecular basis of sickle cell anemia. Be specific
What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.
What qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.
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
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?
The partial pressure of oxygen in the venous blood of a human at rest at sea level is approximately 40 torrs a.) Calculate the fractional saturation of hemoglobin under these conditionsb.) What percentage of the oxygen originally bound to hemoglobin in the alveoli remained unreleased?c.) Is the residual oxygen bound to hemoglobin under these conditions of any benefit? Explain
Which hemoglobin has a higher affinity for O2 at the tissue pO2 of around 4 kPa?
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?
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.
How does the difference between the-chain and the -chain of hemoglobin explain the differences inoxygen binding between Hb A and Hb F?

SEE MORE QUESTIONS

Recommended textbooks for you

Human Physiology: From Cells to Systems (MindTap …

Human Physiology: From Cells to Systems (MindTap …

Biology

ISBN:

9781285866932

Author:

Lauralee Sherwood

Publisher:

Cengage Learning

Human Heredity: Principles and Issues (MindTap Co…

Human Heredity: Principles and Issues (MindTap Co…

Biology

ISBN:

9781305251052

Author:

Michael Cummings

Publisher:

Cengage Learning

Human Physiology: From Cells to Systems (MindTap …

Human Physiology: From Cells to Systems (MindTap …

Biology

ISBN:

9781285866932

Author:

Lauralee Sherwood

Publisher:

Cengage Learning

Human Heredity: Principles and Issues (MindTap Co…

Human Heredity: Principles and Issues (MindTap Co…

Biology

ISBN:

9781305251052

Author:

Michael Cummings

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS