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  2. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    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 ]

  3. Hemoglobin A - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_A

    The most common cause of Hb Bart’s is the inheritance of a deletion allele in that lacks functional α-globin genes from both parents. [9] Hb Bart’s is a tetramer of four gamma-globulin subunits and is ineffective at transporting oxygen to the tissues due to its very high oxygen affinity. [12]

  4. List of human blood components - Wikipedia

    en.wikipedia.org/wiki/List_of_human_blood_components

    0.5-1.5% total Hb smokers, 1-2 packs/day 4-5% total Hb smokers, 2 packs/day 8-9% total Hb toxic >20% total Hb lethal >50% total Hb Carcinoembryonic antigen <2.5 × 10 −9: beta-Carotene: Vitamin A dimer 3-25 × 10 −7: Carotenoids: Antioxidant 2.4-23.1 × 10 −7: Cephalin: 3-11.5 × 10 −4: 0-1 × 10 −4: Ceruloplasmin: 1.5-6 × 10 −4 ...

  5. 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

  6. Ribbon diagram - Wikipedia

    en.wikipedia.org/wiki/Ribbon_diagram

    Ribbon diagram of myoglobin bound to haem (sticks) and oxygen (red spheres) (Ribbon diagrams, also known as Richardson diagrams, are 3D schematic representations of protein structure and are one of the most common methods of protein depiction used today. The ribbon depicts the general course and organization of the protein backbone in 3D and ...

  7. Oxygen–hemoglobin dissociation curve - Wikipedia

    en.wikipedia.org/wiki/Oxygen–hemoglobin...

    Hemoglobin (Hb) is the primary vehicle for transporting oxygen in the blood. Each hemoglobin molecule has the capacity to carry four oxygen molecules. These molecules of oxygen bind to the globin chain of the heme prosthetic group. [1] When hemoglobin has no bound oxygen, nor bound carbon dioxide, it has the unbound conformation (shape). The ...

  8. 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.

  9. File:1GZX Haemoglobin.png - Wikipedia

    en.wikipedia.org/wiki/File:1GZX_Haemoglobin.png

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