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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

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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.
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
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
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
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
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.
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
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
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
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