how to interpret Saturation curves for hemoglobin and myoglobin and how these curves change when allosteric effectors are present.

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.
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how to interpret Saturation curves for hemoglobin and
myoglobin and how these curves change when allosteric effectors
are present.

Expert Solution
Understanding Oxygen dissociation curve

An oxygen dissociation curve is obtained when we plot the %saturation of hemoglobin against the partial pressure of oxygen.

The oxygen dissociation curve represents the affinity and cooperative binding of oxygen to hemoglobin. 

It looks like:

Biochemistry homework question answer, step 1, image 1

So we can see that the affinity for oxygen increases as the pO2 increases. 

The curve is read by looking at the pO2 on x axis and corresponding % saturation value on the Y axis. If 50% saturation is obtained for smaller values of pO2 it means that hemoglobin has more affinity for oxygen. If 50% saturation is not obtained even after increasing the pO2, then hemoglobin has less affinity for oxygen.

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