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  2. Hemoglobin O-Arab - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_O-Arab

    Case reports analysed by Doctor Sayar Dror, [2] PhD, at the Paediatric Hemato-Oncology Unit, “Dana” Children Hospital in Israel, feature three patients; a 12 month-old female of consanguineous parents, a 35 month-old female born to parents known to have the Hemoglobin O-Arab trait, and a 9 month-old male who was asymptomatic and was ...

  3. Hemoglobin variants - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_variants

    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.

  4. List of human blood components - Wikipedia

    en.wikipedia.org/wiki/List_of_human_blood_components

    male >18 yrs 2-30 × 10 −10: female >18 yrs ... Hemoglobin metabolite ... 4.8-6.4 × 10 −5: C7 4.9-7 × ...

  5. Serum iron - Wikipedia

    en.wikipedia.org/wiki/Serum_iron

    Serum iron is a medical laboratory test that measures the amount of circulating iron that is bound to transferrin and freely circulate in the blood. Clinicians order this laboratory test when they are concerned about iron deficiency, which can cause anemia and other problems. 65% of the iron in the body is bound up in hemoglobin molecules in red blood cells.

  6. Glycated hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Glycated_hemoglobin

    Glycated hemoglobin, also called glycohemoglobin, is a form of hemoglobin (Hb) that is chemically linked to a sugar. [ note 1 ] Most monosaccharides , including glucose , galactose , and fructose , spontaneously (that is, non-enzymatically ) bond with hemoglobin when they are present in the bloodstream.

  7. Hemoglobin D - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_D

    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.

  8. Red blood cell - Wikipedia

    en.wikipedia.org/wiki/Red_blood_cell

    Each hemoglobin molecule carries four heme groups; hemoglobin constitutes about a third of the total cell volume. Hemoglobin is responsible for the transport of more than 98% of the oxygen in the body (the remaining oxygen is carried dissolved in the blood plasma). The red blood cells of an average adult human male store collectively about 2.5 ...

  9. Sickle cell disease - Wikipedia

    en.wikipedia.org/wiki/Sickle_cell_disease

    Hemoglobin is extracted from the red cells, then introduced into a porous gel and subjected to an electrical field. This separates the normal and abnormal types of hemoglobin which can then be identified and quantified. [84] Isoelectric focusing (IEF) is a technique that can be used to diagnose sickle cell disease and other hemoglobinopathies.