does BPG bind to deoxyhemoglobin only？why BPG does not bind to oxyhemoglobin？what is chemical structure difference between deoxyhemoglobin and oxyhemoglobin？ #nid100-Percent of saturation50-0-No BPG0₂0B₂With BPGBPG also plays a role in supplying a growing fetus with oxygen. The fetus ob-tains oxygen from the mother's bloodstream via the placenta. Fetal hemoglobin(Hb F) has a higher affinity for oxygen than does maternal hemoglobin, allow-ing for efficient transfer of oxygen from the mother to the fetus (Figure 4.29).BPG80 100206040O₂ pressure (po, in torrs)N+Figure 4.28 A comparison of the oxygen-bindingproperties of hemoglobin in the presence and absenceof BPG. Note that the presence of the BPG markedlydecreases the affinity of hemoglobin for oxygen.enistor to subbun 4-5 Quaternary Structure of Proteins@Percent of saturationB₁on 24 ought 100 Fetal hemoglobin50-1621a10+0Figure 27 The binding of BPG todeoxyhemoglobin. Note the electrostaticintentions between the BPG and the protein.(lisation, Irving Geis. Rights owned by HowardHughes Medical Institute. Not to be reproducedwithout permission.)Maternalhemoglobin97O, flows frommaternaloxyhemoglobinto fetaldeoxyhemoglobin18 AAsimenA Ils obbl2AO₂ pressure (po, in torrs)Figure 4.29 A comparison of the oxygen-binding capacityquepof fetal and maternal hemoglobins. Fetal hemoglobin binds bould hyr si ayawless strongly to BPG and, consequently, has a greater affinityfor oxygen than does maternal hemoglobin.

Hemoglobin is a globular protein, ie it is roughly spherical. It is a tetramer of two types of…

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does BPG bind to deoxyhemoglobin only？why BPG does not bind to oxyhemoglobin？ what is chemical structure difference between deoxyhemoglobin and oxyhemoglobin？

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

46
Hemoglobin A inhibits the formation of the long fibers of hemoglobin S and the subsequent sickling of the red cell on deoxygenation. Why does hemoglobin A have this effect?
Describe how the following allosteric effectors regulated Hemoglobin’s O2 affinity: • CO2• H+ (pH; Explain the basis for the Bohr Effect)• 2,3-BPG • CO
What does the hemoglobin graph regarding YO2 represent?
What other molecules bind to hemoglobin? How do they affect the affinity of Hb for O2?
72.4.1
Under appropriate denaturing conditions, hemoglobin can dissociate into four separate subunits. An isolated alpha subunit binds oxygen, but the O2-saturation curve is hyperbolic rather than sigmoid. In addition, the binding of oxygen to an isolated alpha 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?
7L.4.2
Talk about the factors that can move the oxygen-hemoglobin dissociation curve TO THE RIGHT. What factors move the oxygen-hemoglobin dissociation curve TO THE LEFT? What does this mean, exactly?
What is the equilibrium expression of oxygenated hemoglobin to deoxygenated hemoglobin?
How many heme groups are in hemoglobin and How does oxygen bind to heme?
How different areoxyhemoglobin andhemoglobin? Where is itexpected to find a higherconcentration ofoxyhemoglobin, in peripheraltissues or in the lungs?