Hemoglobinuria Malarial

Hemoglobin in humans is a pigment dye of red blood. The basis of human hemoglobin is a tetramer - hemoglobin A4, consisting of four subunits. Normally, during hemoglobin synthesis, only one subunit contains phenylalanine, but this variant can also lead to a decrease in hemoglobin. However, with hemoglobin A2, the amino acid tyrosine is present in one of the two subunits, and not phenylalane or tryptophan. In iron deficiency anemia, hemoglobin A is most likely synthesized, containing tyrosines in both chains. The function of hemoglobin is the transfer of O2 and CO2, but these molecules of native hemoglobin bind to it more firmly than in modified versions of hemoglobins. Because of this, hemoglobins in the blood come into strong contact with each other with the formation of blood clots - thrombi and red blood cell aggregations. This process leads to impaired circulation, thrombus formation in blood vessels, damage to tissues and organ systems, and their death. This can manifest itself in various symptoms and diseases, among which hemolytic diseases play a special role in pathogenesis.