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Heinz bodies, which may result in hemolytic anemia, can be formed by the following changes to hemoglobin EXCEPT?
A) substitution of proline for residues in alpha helical regions
B) substitutions that affect heme binding
C) substitutions that reduce the affinity of hemoglobin for oxygen
D) substitutions of polar for non-polar residues in the hydrophobic core of hemoglobin

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mfanzorena

Answer:

C) substitutions that reduce the affinity of hemoglobin for oxygen

Explanation:

Heinz bodies are inclusions in the eritrocite, filled by denaturalized globin (protein part of the hemoglobin). Hemoglobin is formed by 4 globin subunits (2 alpha chains and 2 beta chains) plus a heme group. The latter, is responsible for oxygen binding.

The denaturalization of the globin is caused by substitutions that do not allow the protein to fold properly and bind the heme group accordingly. This is the cause of the Heinz bodies in the eritrocite. Therefore, this is a structural problem that impedes the protein to fold into a functional protein and has nothing to do with hemoglobin having less affinity for oxygen. In the last mentioned case, the protein is still functional but poorly binds oxygen, hence, does not for Heinz bodies.

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