loss of only one amino acid from the normal hemoglobin molecule
terminal amino acid of the beta chain
The difference in electrophoretic pattern between normal hemoglobin A and hemoglobin S is due to a single amino acid substitution. In hemoglobin S, a glutamic acid is replaced by a valine at position 6 of the beta-globin chain. This change causes hemoglobin S to have a different charge, leading to its characteristic migration pattern on electrophoresis.
Sickle cell hemoglobin differs from normal hemoglobin due to a mutation in the gene that codes for the hemoglobin protein. This mutation leads to the production of an abnormal hemoglobin variant (HbS) that causes red blood cells to become sickle-shaped, leading to various complications such as blockages in blood vessels and reduced oxygen delivery to tissues.
The pro of sickle cell hemoglobin is that if you have only one allele for sickle cell hemoglobin and the other allele is normal, then you are immune to malaria.
Hemoglobin
It is Hemoglobin
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The difference is that a patient with sickle cell disease has an increased level of one specific type of Hemoglobin, that is Fetal hemoglobin or HbF. However, the amount of total hemoglobin is the same.
The condition is called sickle cell trait. This occurs when an individual inherits one sickle cell gene and one normal hemoglobin gene, resulting in milder symptoms compared to sickle cell disease.
Sickle-cell anemia
The amino acid sequence of the sickle cell allele for hemoglobin varies from the normal allele for hemoglobin by one amino acid. The sickle cell allele for hemoglobin has valine instead of glutamic acid. When the oxygen level of the blood decreases, the hemoglobin molecules come out of solution, stick together, and form long chains that cause the red blood cells to become sickle shaped.