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There are two types of Alpha-thalassemia, named hemoglobin Bart hydrops fetalis syndrome (also known as Hb Bart syndrome) and HbH disease. [22] Anemia: D50-D64: 663: Anemia is a type of medical condition that results in a decrease in the number of red blood cells (RBCs) or less than the normal quantity of hemoglobin in the blood. [2] Anemia of ...
Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers an animal's metabolism. A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and ...
Unstable hemoglobin variants are mutations that cause the hemoglobin molecule to precipitate, spontaneously or upon oxidative stress, resulting in hemolytic anemia. Precipitated, denatured hemoglobin can attach to the inner layer of the plasma membrane of the red blood cell (RBC) forming Heinz bodies , leading to premature destruction of the ...
Hemoglobin A (HbA), also known as adult hemoglobin, hemoglobin A1 or α 2 β 2, is the most common human hemoglobin tetramer, accounting for over 97% of the total red blood cell hemoglobin. [1] Hemoglobin is an oxygen-binding protein, found in erythrocytes , which transports oxygen from the lungs to the tissues. [ 2 ]
Hemoglobin variants occur when there are mutations in specific genes that code for the protein chains, known as globins, which make up the hemoglobin molecule. This leads to amino acid substitutions in the hemoglobin molecule that could affect the structure, properties, and/or the stability of the hemoglobin molecule.
Hemoglobin Barts, abbreviated Hb Barts, is an abnormal type of hemoglobin that consists of four gamma globins. It is moderately insoluble, and therefore accumulates in the red blood cells. Hb Barts has an extremely high affinity for oxygen, so it cannot release oxygen to the tissue. Therefore, this makes it an inefficient oxygen carrier.
The hemoglobin was named hemoglobin III, [24] but hemoglobin C was eventually used. [ 25 ] [ 26 ] By 1954, it was found that the mutant hemoglobin was highly prevalent in West Africa. [ 27 ] [ 28 ] In 1960, Vernon Ingram and J. A. Hunt at the University of Cambridge discovered that the mutation was a single amino acid replacement of glutamic ...
Hemoglobin D has the basic structure and composition of normal adult hemoglobin. It is a globular protein containing prosthetic (non-protein) group called heme. There are four individual peptide chains, namely two α- and two β-subunits, each made of 141 and 146 amino acid residues, respectively.