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Red blood cells synthesize and degrade 2,3-biphosphogylerate (2,3-BPG) as a detour from the glycolytic pathway, as shown in the figure. 2,3-BPG decreases the oxygen affinity of hemoglobin by binding in the central cavity of the deoxygenated form of hemoglobin. This encourages delivery of oxygen to tissues. A defect in one of the glycolytic enzymes may affect levels of 2,3-BPG. The plot above right shows oxygen-binding curves for normal erythrocytes and for hexokinase and pyruvate kinase-deficient erythrocytes. Identify which curve corresponds to which enzyme deficiency.

Red blood cells synthesize and degrade 2,3-biphosphogylerate (2,3-BPG) as a detour from the glycolytic pathway, as shown in the figure. 2,3-BPG decreases the oxygen affinity of hemoglobin by binding in the central cavity of the deoxygenated form of hemoglobin. This encourages delivery of oxygen to tissues. A defect in one of the glycolytic enzymes may affect levels of 2,3-BPG. The plot above right shows oxygen-binding curves for normal erythrocytes and for hexokinase and pyruvate kinase-deficient erythrocytes. Identify which curve corresponds to which enzyme deficiency.

Biochemistry
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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Red blood cells synthesize and degrade 2,3-biphosphogylerate (2,3-BPG) as a detour from the glycolytic pathway, as shown in the figure.

2,3-BPG decreases the oxygen affinity of hemoglobin by binding in the central cavity of the deoxygenated form of hemoglobin. This encourages delivery of oxygen to tissues. A defect in one of the glycolytic enzymes may affect levels of 2,3-BPG. The plot above right shows oxygen-binding curves for normal erythrocytes and for hexokinase and pyruvate kinase-deficient erythrocytes. Identify which curve corresponds to which enzyme deficiency.

20. Red blood cells synthesize and degrade 2,3-bisphosphoglyc- erate (2,3-BPG) as a detour from the glycolytic pathway, as shown in the figure. Glyceraldehyde-3-P GAPDH 1,3-Bisphosphoglycerate 1|PGK 3-Phosphoglycerate 2,3-Bisphosphoglycerate 2,3-BPG decreases the oxygen affinity of hemoglobin by binding in the central cavity of the deoxygenated form of hemoglobin. This encourages delivery of oxygen to tissues. A defect in one of the gly- colytic enzymes may affect levels of 2,3-BPG. The plot above right shows oxygen-binding curves for normal erythrocytes and for hexo- kinase- and pyruvate kinase-deficient erythrocytes. Identify which curve corresponds to which enzyme deficiency,
Transcribed Image Text:20. Red blood cells synthesize and degrade 2,3-bisphosphoglyc- erate (2,3-BPG) as a detour from the glycolytic pathway, as shown in the figure. Glyceraldehyde-3-P GAPDH 1,3-Bisphosphoglycerate 1|PGK 3-Phosphoglycerate 2,3-Bisphosphoglycerate 2,3-BPG decreases the oxygen affinity of hemoglobin by binding in the central cavity of the deoxygenated form of hemoglobin. This encourages delivery of oxygen to tissues. A defect in one of the gly- colytic enzymes may affect levels of 2,3-BPG. The plot above right shows oxygen-binding curves for normal erythrocytes and for hexo- kinase- and pyruvate kinase-deficient erythrocytes. Identify which curve corresponds to which enzyme deficiency,
Oxygen saturation (%) 100 90 80 70 60 - Normal 50 40 30 20 10 0 0 10 20 30 40 50 60 po₂ (torr) erythrocytes
Transcribed Image Text:Oxygen saturation (%) 100 90 80 70 60 - Normal 50 40 30 20 10 0 0 10 20 30 40 50 60 po₂ (torr) erythrocytes
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