From the figure of O2 binding to myoglobin and hemoglobin (ignore the line marked as T) as described in lecture (shown below) answer the following questions. a) Estimate the P50 for myoglobin from the plot. Show how this estimation is determined from the binding curve above. ( The first ghraph) b)Using YO2 = PO2/P50 + PO2 , calculate the fraction of O2 bound for myoglobin at 1 torr. (2nd graph) c)Using the binding curve on the previous page, show how you can estimate what fraction of hemoglobin is bound near tissues at a pO2 of 30 torr and provide this value. If the pH were lowered, will the amount of O2 bound to hemoglobin at 30 torr increase or decrease? Explain why this is so based on how this changes hemoglobin structure. If 2,3-BPG were added to the solution, will the amount of O2 bound to hemoglobin at 30 torr increase or decrease? Explain why this is so based on how this changes hemoglobin structure.
From the figure of O2 binding to myoglobin and hemoglobin (ignore the line
marked as T) as described in lecture (shown below) answer the following questions.
a) Estimate the P50 for myoglobin from the plot. Show how this estimation is
determined from the binding curve above. ( The first ghraph)
b)Using YO2 = PO2/P50 + PO2 , calculate the fraction of O2 bound for myoglobin at 1 torr. (2nd graph)
c)Using the binding curve on the previous page, show how you can estimate what
fraction of hemoglobin is bound near tissues at a pO2 of 30 torr and provide this value.
If the pH were lowered, will the amount of O2 bound to hemoglobin at 30 torr increase
or decrease? Explain why this is so based on how this changes hemoglobin structure.
If 2,3-BPG were added to the solution, will the amount of O2 bound to hemoglobin at
30 torr increase or decrease? Explain why this is so based on how this changes hemoglobin
structure.
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