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Hemoglobin (haemoglobin, [a] Hb or Hgb) is a protein containing iron that facilitates the transportation of oxygen in red blood cells. Almost all vertebrates contain hemoglobin, [ 3 ] with the sole exception of the fish family Channichthyidae . [ 4 ]
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HB SS which is the most common and severe form of sickle cell. Hb SC is due to inheriting Hb S from one parent and Hb C (hemoglobin C) from the other parent. Hb S beta thalassemia is the least common and is experienced in patients who have inherited beta thalassemia hemoglobin from one parent and HbS from the other. [17]
Some normal hemoglobin types are; Hemoglobin A (Hb A), which is 95–98% of hemoglobin found in adults, Hemoglobin A2 (Hb A2), which is 2–3% of hemoglobin found in adults, and Hemoglobin F (Hb F), which is found in adults up to 2.5% and is the primary hemoglobin that is produced by the fetus during pregnancy.
Hemoglobin C (abbreviated as HbC) is an abnormal hemoglobin in which glutamic acid residue at the 6th position of the β-globin chain is replaced with a lysine residue due to a point mutation in the HBB gene. [1]
The structure of Hb A consists of two α-globin chains bound to two β-globin chains to form a tetramer (a protein made up four protein chains). [3] When there is lower than normal production of α-globin, as in Hb H disease, the excess β-globin form β4-tetramers, termed Hemoglobin H.
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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.