1. The most rapid way that erythrocytes adapt to high altitudes is
   A
   Option A: by producing genetically altered hemoglobins that have higher O2-binding affinities.
   B
   Option B: by increasing the concentration of hemoglobin.
   C
   Option C: by relying upon the simpler protein myoglobin.
   D
   Option D: by adopting the symmetry model of allosterism.
   E
   Option E: by increasing the intracellular concentration of BPG.

Option E: by increasing the intracellular concentration of BPG.

2. Which of the following increases the affinity of hemoglobin for O2?
   A
   Option A: a decrease in pH
   B
   Option B: an increase in pH
   C
   Option C: an increase in CO2 concentration
   D
   Option D: the formation of N-terminal carbamates
   E
   Option E: an increase in BPG concentration

Option B: an increase in pH

3. The Bohr effect refers to
   A
   Option A: the decrease in affinity of Hb for O2 when the BPG concentration goes down
   B
   Option B: the decrease in affinity of Hb for O2 when the pH goes down
   C
   Option C: the decrease in affinity of Hb for O2 when the pH goes up
   D
   Option D: the increase in the affinity of Hb for O2 when the O2 concentration goes up
   E
   Option E: the decrease in affinity of Hb for O2 when the BPG concentration goes up

Option B: the decrease in affinity of Hb for O2 when the pH goes down

4. While the binding of O2 to myoglobin as a function of pO2 is described by a simple __________ curve, the binding to hemoglobin is described by a more complex ______ curve.
   A
   Option A: sigmoidal; hyperbolic
   B
   Option B: sigmoidal; bell-shaped
   C
   Option C: hyperbolic; sigmoidal
   D
   Option D: exponential; hyperbolic
   E
   Option E: hyperbolic; concave

Option C: hyperbolic; sigmoidal

5. The Hill plot shows that the fourth oxygen binds to hemoglobin with a ______-fold greater affinity than the first.
   A
   Option A: 10
   B
   Option B: 20
   C
   Option C: 2
   D
   Option D: 100
   E
   Option E: 5

Option D: 100

6. Consider a hypothetical hemoglobin-like molecule with a Hill coefficient (constant) of 1 and the same p50 value as normal hemoglobin. Choose the statement below that best describes the two proteins.
   A
   Option A: There is a cooperative interaction between oxygen-binding sites in both the hypothetical and normal hemoglobins.
   B
   Option B: The oxygen binding curve for the hypothetical hemoglobin is hyperbolic, and the curve for normal hemoglobin is sigmoidal.
   C
   Option C: The hypothetical hemoglobin has a greater oxygen affinity than normal hemoglobin.
   D
   Option D: At pO2 less than p50, normal hemoglobin has a greater YO2 value.
   E
   Option E: The two hemoglobins would be able to deliver about the same amount of oxygen to the tissues.

Option B: The oxygen binding curve for the hypothetical hemoglobin is hyperbolic, and the curve for normal hemoglobin is sigmoidal.

7. The value of n, the Hill constant (coefficient), for hemoglobin is about ______ as great as the value for myoglobin.
   A
   Option A: twice
   B
   Option B: ten times
   C
   Option C: half
   D
   Option D: three times
   E
   Option E: five times

Option D: three times

8. Hemoglobin's p50 value is about ______ as great as myoglobin's p50 value.
   A
   Option A: one-tenth
   B
   Option B: twice
   C
   Option C: twenty times
   D
   Option D: half
   E
   Option E: ten times

Option E: ten times

9. When the partial pressure of O2 in venous blood is 30 torr, the saturation of myoglobin with O2 is ______ while the saturation of hemoglobin with O2 is ______.
   A
   Option A: 0.55, 0.91
   B
   Option B: 0.91, 0.55
   C
   Option C: none of the above
   D
   Option D: 2.8 torr, 26 torr
   E
   Option E: 0.91, 0.97

Option B: 0.91, 0.55

10. The oxygen binding by hemocyanins is mediated by
    A
    Option A: a copper atom
    B
    Option B: a pair of iron ions
    C
    Option C: a pair of copper atoms
    D
    Option D: a heme group
    E
    Option E: an iron ion

Option C: a pair of copper atoms