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  2. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers an animal's metabolism. A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and ...

  3. Globin - Wikipedia

    en.wikipedia.org/wiki/Globin

    The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular event that gives rise to sickle-cell disease .

  4. Hemoglobin A - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_A

    Globin synthesis takes place in the ribosomes which are located within the cytosol. Two globin chains that have heme groups combine to form hemoglobin. One of the chains is an alpha chain and the other is a non-alpha chain. Non-alpha chain nature in hemoglobin molecules varies due to different variables.

  5. Hemoglobin subunit beta - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_subunit_beta

    Hemoglobin subunit beta (beta globin, β-globin, haemoglobin beta, hemoglobin beta) is a globin protein, coded for by the HBB gene, which along with alpha globin , makes up the most common form of haemoglobin in adult humans, hemoglobin A (HbA). [5] It is 147 amino acids long and has a molecular weight of 15,867 Da.

  6. Respiratory pigment - Wikipedia

    en.wikipedia.org/wiki/Respiratory_pigment

    Hemoglobin A is the “normal” hemoglobin, the variant of hemoglobin that is most common after birth. Hemoglobin A2 is a minor component of hemoglobin found in red blood cells. Hemoglobin A2 makes up less than 3% of total red blood cell hemoglobin. Hemoglobin F typically is only found in the fetal stage of development.

  7. Blood - Wikipedia

    en.wikipedia.org/wiki/Blood

    Hemoglobin, the main oxygen-carrying molecule in red blood cells, carries both oxygen and carbon dioxide. However, the CO 2 bound to hemoglobin does not bind to the same site as oxygen. Instead, it combines with the N-terminal groups on the four globin chains.

  8. Globular protein - Wikipedia

    en.wikipedia.org/wiki/Globular_protein

    Among the most known globular proteins is hemoglobin, a member of the globin protein family. Other globular proteins are the alpha, beta and gamma (IgA, IgD, IgE, IgG and IgM) globulin. See protein electrophoresis for more information on the different globulins.

  9. 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 ...