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At pH 7.2 and 10 Torr oxygen partial pressure, the extent of O2 binding is:
- a)High for both hemoglobin and myoglobin
- b)High for hemoglobin and low for myoglobin
- c)High for myoglobin and low for hemoglobin
- d)Low for both hemoglobin and myoglobin
Correct answer is option 'C'. Can you explain this answer?
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At pH 7.2 and 10 Torr oxygen partial pressure, the extent of O2 bindin...
PH and Oxygen Partial Pressure and their effect on O2 binding
pH and oxygen partial pressure are two important factors that affect the binding of oxygen to hemoglobin and myoglobin. Hemoglobin and myoglobin are both proteins involved in oxygen transport and storage in the body.
pH: pH is the measure of acidity or basicity of a solution. The pH of blood is tightly regulated within a narrow range of 7.35-7.45. Any change in pH can affect the binding of oxygen to hemoglobin and myoglobin.
Oxygen Partial Pressure: Oxygen partial pressure is the measure of the concentration of oxygen in a mixture of gases. It is expressed in Torr or mmHg. The oxygen partial pressure in arterial blood is around 100 Torr.
Extent of O2 Binding at pH 7.2 and 10 Torr oxygen partial pressure
At pH 7.2 and 10 Torr oxygen partial pressure, the extent of O2 binding is high for myoglobin and low for hemoglobin. This is because:
- Myoglobin has a higher affinity for oxygen than hemoglobin at low oxygen partial pressures. This means that myoglobin can bind oxygen more easily than hemoglobin at low oxygen concentrations.
- At pH 7.2, the affinity of myoglobin for oxygen is further increased due to the Bohr effect. The Bohr effect is a phenomenon where the binding of oxygen to hemoglobin and myoglobin is influenced by the pH of the blood. At low pH, the affinity of myoglobin for oxygen is increased due to the release of protons, which stabilizes the T state of myoglobin and facilitates oxygen binding.
- Hemoglobin, on the other hand, has a lower affinity for oxygen at low oxygen partial pressures. This is because hemoglobin undergoes a conformational change from the T state to the R state upon binding to oxygen. This conformational change is facilitated by the release of protons, which is why hemoglobin has a higher affinity for oxygen at high pH.
Therefore, at pH 7.2 and 10 Torr oxygen partial pressure, myoglobin binds oxygen more easily than hemoglobin.
pH and oxygen partial pressure are two important factors that affect the binding of oxygen to hemoglobin and myoglobin. Hemoglobin and myoglobin are both proteins involved in oxygen transport and storage in the body.
pH: pH is the measure of acidity or basicity of a solution. The pH of blood is tightly regulated within a narrow range of 7.35-7.45. Any change in pH can affect the binding of oxygen to hemoglobin and myoglobin.
Oxygen Partial Pressure: Oxygen partial pressure is the measure of the concentration of oxygen in a mixture of gases. It is expressed in Torr or mmHg. The oxygen partial pressure in arterial blood is around 100 Torr.
Extent of O2 Binding at pH 7.2 and 10 Torr oxygen partial pressure
At pH 7.2 and 10 Torr oxygen partial pressure, the extent of O2 binding is high for myoglobin and low for hemoglobin. This is because:
- Myoglobin has a higher affinity for oxygen than hemoglobin at low oxygen partial pressures. This means that myoglobin can bind oxygen more easily than hemoglobin at low oxygen concentrations.
- At pH 7.2, the affinity of myoglobin for oxygen is further increased due to the Bohr effect. The Bohr effect is a phenomenon where the binding of oxygen to hemoglobin and myoglobin is influenced by the pH of the blood. At low pH, the affinity of myoglobin for oxygen is increased due to the release of protons, which stabilizes the T state of myoglobin and facilitates oxygen binding.
- Hemoglobin, on the other hand, has a lower affinity for oxygen at low oxygen partial pressures. This is because hemoglobin undergoes a conformational change from the T state to the R state upon binding to oxygen. This conformational change is facilitated by the release of protons, which is why hemoglobin has a higher affinity for oxygen at high pH.
Therefore, at pH 7.2 and 10 Torr oxygen partial pressure, myoglobin binds oxygen more easily than hemoglobin.
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At pH 7.2 and 10 Torr oxygen partial pressure, the extent of O2 bindin...
HB IS PH DEPNDENT WHILE MB IS PH INDEPNDENT..
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At pH 7.2 and 10 Torr oxygen partial pressure, the extent of O2 binding is:a)High for both hemoglobin and myoglobinb)High for hemoglobin and low for myoglobinc)High for myoglobin and low for hemoglobind)Low for both hemoglobin and myoglobinCorrect answer is option 'C'. Can you explain this answer?
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