Hemoglobins. Eryhem . Ferrous Hemoglobin . Hemoglobin . Hemoglobin, Ferrous . The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. . 1.00
Hemoglobin A. Normal adult human hemoglobin. The globin moiety consists of two alpha and two beta chains. . 0.88
Hemoglobinuria. The presence of free HEMOGLOBIN in the URINE, indicating hemolysis of ERYTHROCYTES within the vascular system. After saturating the hemoglobin-binding proteins (HAPTOGLOBINS), free hemoglobin begins to appear in the urine. . 0.86
Hemoglobin, Sickle. Deoxygenated Sickle Hemoglobin . Deoxyhemoglobin S . Hemoglobin SS . Hemoglobin, Deoxygenated Sickle . SS, Hemoglobin . Sickle Hemoglobin . Sickle Hemoglobin, Deoxygenated . Hemoglobin S . An abnormal hemoglobin resulting from the substitution of valine for glutamic acid at position 6 of the beta chain of the globin moiety. The heterozygous state results in sickle cell trait, the homozygous in sickle cell anemia. . 0.84
Hemoglobin C. A commonly occurring abnormal hemoglobin in which lysine replaces a glutamic acid residue at the sixth position of the beta chains. It results in reduced plasticity of erythrocytes. . 0.83
Hemoglobin E. An abnormal hemoglobin that results from the substitution of lysine for glutamic acid at position 26 of the beta chain. It is most frequently observed in southeast Asian populations. . 0.81
Hemoglobin H. An abnormal hemoglobin composed of four beta chains. It is caused by the reduced synthesis of the alpha chain. This abnormality results in ALPHA-THALASSEMIA. . 0.80
