Chapter 10 - Hemoglobin Metabolism Flashcards

1
Q

A hemoglobin molecule is composed of:

A

d. Four heme molecules and four globin chains

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2
Q

Normal adult Hb A contains which polypeptide chains?

A

a. α and β

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3
Q

A key rate-limiting step in heme synthesis is suppression of:

A

a. Aminolevulinate synthase

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4
Q

Which of the following forms of hemoglobin molecule has the lowest affinity for oxygen?

A

a. Tense

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5
Q

Using the normal hemoglobin-oxygen dissociation curve in Figure 10-7 for reference, predict the position of the curve when there is a decrease in pH.

A

a. Shifted to the right of normal with decreased oxygen affinity

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6
Q

The predominant hemoglobin found in a healthy newborn is:

A

d. F

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7
Q

What is the normal distribution of hemoglobins in healthy adults?

A

c. .95% Hb A, ,3.5% Hb A2, 1% to 2% Hb F

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8
Q

Which of the following is a description of the structure of
oxidized hemoglobin?

A

b. Hemoglobin with iron in the ferric state (methemoglobin) and not able to carry oxygen

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9
Q

In the quaternary structure of hemoglobin, the globin
chains associate into:

A

d. Two αβ dimers

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10
Q

How are the globin chain genes arranged?

A

b. With α genes and β genes on separate chromosomes, including two a genes on one chromosome and one β gene on a different chromosome

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11
Q

The nature of the interaction between 2,3-BPG and hemoglobin is that 2,3-BPG

A

c. Binds to amino acids of the globin chain, contributing to a conformational change that inhibits oxygen from binding to heme

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