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Question

Sickle cell anemia is caused by

A
Complete absence of the haemoglobin gene
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B
Point mutation of the haemoglobin gene
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C
Increased affinity of haemoglobin for oxygen
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D
Truncation of the haemoglobin protein
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Solution

The correct option is B Point mutation of the haemoglobin gene
Hemoglobin has four protein subunits, two α-globin and two β-globin. The Hbb gene codes the β chain. A missense mutation, replacement of A by T at the 17th nucleotide of the Hbb gene changes the codon GAG (glutamic acid) to GTG (which encodes valine). Thus, the disease is caused by a point mutation (change in single nucleotide base) in the gene; option B is correct.
The mutations that introduce a stop codon in between the reading frame causing premature termination of protein synthesis results in truncated protein; options A and D are incorrect as there is the substitution of amino acids, no premature termination or complete suppression of haemoglobin synthesis. The mutated allele Hbs encodes the abnormal haemoglobin molecules which stick to one another and cause stiffness and sickle shape of red blood cells. The sickle-shaped RBCs block and damage the vital organs and tissue; they do not show an altered affinity for oxygen, option C is incorrect.

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