Oxygen binding is monitored for a solution of hemoglobin. During the experiment, the curve changes from sigmoidal to hyperbolic. Which of the following may be the reason for the change?
Added by Elaine P.
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This is typical for normal hemoglobin, where the curve represents cooperative binding, meaning that the binding of one oxygen molecule facilitates the binding of subsequent oxygen molecules. Show more…
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A right shift in the Oxy-Hb dissociation curve means that hemoglobin has a lower affinity for oxygen relative to a normal curve. It occurs under the conditions of exercise, including increased temperature and lower pH. This shift results from slight changes in the shape of the hemoglobin protein (quaternary structure) that occur because of changes in the interactions of the amino acid side chains when temperature is increased or pH is reduced, among other causes. Therefore, the correct answer is d.) all of the above.
Adi S.
Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated $\alpha$ subunit binds oxygen, but the O_2-saturation curve is hyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated $a$ subunit is not affected by the presence of $\mathrm{H}^{+}, \mathrm{CO}_{2}$, or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?
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