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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. Hemoglobin A - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_A

    The structure of adult human hemoglobin. α and β subunits are shown in red and blue, and the iron-containing heme groups in green. From PDB: 1GZX Proteopedia Hemoglobin. Hemoglobin A (HbA), also known as adult hemoglobin, hemoglobin A1 or α 2 β 2, is the most common human hemoglobin tetramer, accounting for over 97% of the total red blood ...

  4. Blood cell - Wikipedia

    en.wikipedia.org/wiki/Blood_cell

    Red blood cells or erythrocytes primarily carry oxygen and collect carbon dioxide through the use of hemoglobin. [2] Hemoglobin is an iron-containing protein that gives red blood cells their color and facilitates transportation of oxygen from the lungs to tissues and carbon dioxide from tissues to the lungs to be exhaled. [3]

  5. 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 ...

  6. Blood - Wikipedia

    en.wikipedia.org/wiki/Blood

    Hemoglobin has an oxygen binding capacity between 1.36 and 1.40 ml O 2 per gram hemoglobin, [23] which increases the total blood oxygen capacity seventyfold, [24] compared to if oxygen solely were carried by its solubility of 0.03 ml O 2 per liter blood per mm Hg partial pressure of oxygen (about 100 mm Hg in arteries). [24]

  7. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    For example, the ability of hemoglobin to effectively deliver oxygen to tissues is due to specific amino acid residues located near the heme molecule. [13] Hemoglobin reversibly binds to oxygen in the lungs when the pH is high, and the carbon dioxide concentration is low. When the situation is reversed (low pH and high carbon dioxide ...

  8. List of human blood components - Wikipedia

    en.wikipedia.org/wiki/List_of_human_blood_components

    Hemoglobin metabolite 2-14 × 10 −6: 1-10 × 10 −6: Biotin (Vitamin H) Gluconeogenesis, metabolize leucine, fatty acid synthesis 7-17 × 10 −9: 9-16 × 10 −9: Blood Urea Nitrogen (BUN) 8-23 × 10 −5: Bradykinin: 7 × 10 −11: Bromide: 7-10 × 10 −9: Cadmium: normal 1-5 × 10 −9: toxic 0.1-3 × 10 −6: Calciferol (vitamin D 2 ...

  9. 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 organisation of the protein backbone in 3D and ...