True or False: The low pH of blood in the lungs causes a shift in oxygen's binding to hemoglobin favoring its release.

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
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**Question:** True or False: The low pH of blood in the lungs causes a shift in oxygen’s binding to hemoglobin favoring its release.

**Explanation:** 
- This statement is related to the Bohr effect, which describes how changes in pH and carbon dioxide concentration affect hemoglobin’s affinity for oxygen.
- At lower pH levels, which are often found in actively metabolizing tissues (not the lungs), hemoglobin tends to release oxygen more readily to support cellular respiration.
- In the lungs, the pH is usually higher, facilitating the uptake of oxygen by hemoglobin. Therefore, the statement might be misleading. The release of oxygen occurs more efficiently in tissues with low pH, not in the lungs.  

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Transcribed Image Text:**Question:** True or False: The low pH of blood in the lungs causes a shift in oxygen’s binding to hemoglobin favoring its release. **Explanation:** - This statement is related to the Bohr effect, which describes how changes in pH and carbon dioxide concentration affect hemoglobin’s affinity for oxygen. - At lower pH levels, which are often found in actively metabolizing tissues (not the lungs), hemoglobin tends to release oxygen more readily to support cellular respiration. - In the lungs, the pH is usually higher, facilitating the uptake of oxygen by hemoglobin. Therefore, the statement might be misleading. The release of oxygen occurs more efficiently in tissues with low pH, not in the lungs. No graphs or diagrams are present in the image.
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Hemoglobin is a transport protein found in the blood that transports oxygen from the lungs to various tissues of the body. Hemoglobin is found inside the RBCs or red blood cells. Hemoglobin is a tetrameric protein with two alpha and two beta polypeptide chains. Each polypeptide chain contains a single oxygen binding site. 

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