Dissociation Curves
We can compare compare the binding properties of both myoglobin and hemoglobin by drawing their dissociation curves. These curves measure their relative affinities for oxygen.
- We draw a graph and label the x-axis oxygen partial pressure (torr). Number it 0 to 120.
– 30 torr is ~ the partial pressure of oxygen in the body's tissues.
– 100 torr is ~ the partial pressure in the lungs.
- The y-axis % oxygen saturation: it's numbered 0 to 100.
We will use it to compare the oxygen binding patterns of both hemoglobin and myoglobin.
oxygen binding curve for hemoglobin and myoglobin
Hemoglobin
- We draw a sigmoidal curve that plateaus just below 100% saturation.
- Cooperative binding produces this sigmoidal shape.
– As one oxygen molecule binds, hemoglobin's affinity for additional oxygen increases, and its percent saturation rapidly increases.
- We show that hemoglobin reaches half saturation in the peripheral tissues – it responds to oxygen availability and releases it when partial pressure is low.
Myoglobin
- We draw a hyperbolic curve to the left of the hemoglobin curve, a much simpler binding pattern that corresponds to myoglobin's single heme group.
– Myoglobin has a high affinity for oxygen, and does not release it until the partial pressure is very low.
– These binding properties correspond to myoglobin's role in oxygen storage.
– We label the early portion of the curve "Exercising muscle" and the plateau "Muscle at rest."
Myoglobin vs. Hemoglobin
- Myoglobin releases oxygen in response to the muscle's immediate needs.
- Hemoglobin's cooperative binding allows it to respond to changes in oxygen availability.
Fetal hemoglobin dissociation curve
- As a clinical correlation, we show that the fetal hemoglobin dissociation curve is to the left of the adult hemoglobin curve.
- This is because it has a greater affinity for oxygen to facilitate oxygen transfer from the maternal hemoglobin to the fetus; fetal oxygen supplies come from the mother.