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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. Red blood cell - Wikipedia

    en.wikipedia.org/wiki/Red_blood_cell

    Each human red blood cell contains approximately 270 million hemoglobin molecules. [3] The cell membrane is composed of proteins and lipids, and this structure provides properties essential for physiological cell function such as deformability and stability of the blood cell while traversing the circulatory system and specifically the capillary ...

  5. Blood cell - Wikipedia

    en.wikipedia.org/wiki/Blood_cell

    Red blood cells or erythrocytes pors 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]

  6. 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.

  7. Oxygen–hemoglobin dissociation curve - Wikipedia

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

    The oxygen–hemoglobin dissociation curve, also called the oxyhemoglobin dissociation curve or oxygen dissociation curve (ODC), is a curve that plots the proportion of hemoglobin in its saturated (oxygen-laden) form on the vertical axis against the prevailing oxygen tension on the horizontal axis. This curve is an important tool for ...

  8. Respiratory pigment - Wikipedia

    en.wikipedia.org/wiki/Respiratory_pigment

    Vertebrates use a tetrameric hemoglobin, carried in red blood cells, to breathe. There are multiple types of hemoglobin that have been found in the human body alone. 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.

  9. Globular protein - Wikipedia

    en.wikipedia.org/wiki/Globular_protein

    3-dimensional structure of hemoglobin, a globular protein.. In biochemistry, globular proteins or spheroproteins are spherical ("globe-like") proteins and are one of the common protein types (the others being fibrous, disordered and membrane proteins).