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Oxygen-Hemoglobin Dissociation Curve
Jul 25, 2024
Oxygen-Hemoglobin Dissociation Curve
Overview
Focuses on understanding the oxygen-hemoglobin dissociation or saturation curve.
Discusses the properties of red blood cells and hemoglobin.
Explains factors affecting the dissociation curve.
Red Blood Cells (RBC) Basics
Structure
: Biconcave disc, no nucleus.
Energy Source
: Glycolysis (converts glucose to pyruvate, produces ATP).
Protein Content
: Up to 270 million hemoglobin molecules per RBC.
Hemoglobin Structure
Subunits
: 4 (α1, α2, β1, β2).
Oxygen Binding
: Cooperative binding (allosteric binding) increases affinity with each successive oxygen molecule.
Oxygen-Hemoglobin Dissociation Curve
Axes
: Y-axis = Percent saturation of hemoglobin, X-axis = Partial pressure of oxygen (mm Hg).
Key Points
:
Lungs (105 mm Hg, 98.5% saturation).
Tissue level (40 mm Hg, 75% saturation).
Oxygen Unloading
: At tissue level, roughly 23% of oxygen is released from hemoglobin.
Factors Affecting the Curve
Rightward Shift (CADET mnemonic)
:
Carbon Dioxide (COâ‚‚)
Acidity
2-3 Bisphosphoglycerate (BPG)
Exercise
Temperature
Impact of Rightward Shift
:
Decrease in saturation at tissue level (50% saturation at 40 mm Hg).
Increased oxygen delivery to tissues (48% of available oxygen).
Leftward Shift
Conditions
:
Decrease in COâ‚‚, acidity, temperature, and 2-3 BPG.
Associated with sedentary, cold conditions.
Impact of Leftward Shift
:
Higher saturation at tissue level (85% saturation at 40 mm Hg).
Decreased oxygen delivery (13% of available oxygen).
Fetal Hemoglobin
Characteristics
: Higher affinity for oxygen, shifts curve to the left.
Importance
: Allows efficient transfer of oxygen from mother to fetus through the placenta.
Conclusion
The oxygen-hemoglobin dissociation curve is dynamic and adapts to physiological conditions.
Understanding the curve is crucial for grasping how oxygen is delivered to tissues under different conditions.
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