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Multiple Choice
Which of the following molecules alters the oxygen affinity of hemoglobin?
A
Glucose
B
Cholesterol
C
Urea
D
2,3-Bisphosphoglycerate (2,3-BPG)
Verified step by step guidance
1
Understand the role of hemoglobin in oxygen transport: Hemoglobin is a protein in red blood cells responsible for binding oxygen in the lungs and releasing it in tissues. Its oxygen affinity can be modulated by various molecules.
Learn about 2,3-Bisphosphoglycerate (2,3-BPG): 2,3-BPG is a small molecule produced in red blood cells during glycolysis. It binds to hemoglobin and stabilizes the T-state (tense state), which has a lower affinity for oxygen, facilitating oxygen release to tissues.
Compare the listed molecules: Glucose, cholesterol, and urea do not directly interact with hemoglobin to alter its oxygen affinity. Glucose is a sugar used for energy, cholesterol is a lipid involved in membrane structure, and urea is a waste product of nitrogen metabolism.
Recognize the physiological importance of 2,3-BPG: In conditions like high altitude or hypoxia, 2,3-BPG levels increase to enhance oxygen delivery to tissues by reducing hemoglobin's oxygen affinity.
Conclude that 2,3-BPG is the correct answer: Based on its specific interaction with hemoglobin and its role in modulating oxygen affinity, 2,3-BPG is the molecule that alters hemoglobin's oxygen affinity.