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  2. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    Hemoglobin has an oxygen-binding capacity of 1.34 mL of O 2 per gram, [6] which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. [7] The mammalian hemoglobin molecule can bind and transport up to four oxygen molecules. [8] Hemoglobin also transports other gases.

  3. Dioxygen in biological reactions - Wikipedia

    en.wikipedia.org/wiki/Dioxygen_in_biological...

    In blood, the heme group of hemoglobin binds oxygen when it is present, changing hemoglobin's color from bluish red to bright red. [7] [8] Vertebrate animals use hemoglobin in their blood to transport oxygen from their lungs to their tissues, but other animals use hemocyanin (molluscs and some arthropods) or hemerythrin (spiders and lobsters).

  4. Cellular respiration - Wikipedia

    en.wikipedia.org/wiki/Cellular_respiration

    Although cellular respiration is technically a combustion reaction, it is an unusual one because of the slow, controlled release of energy from the series of reactions. Nutrients that are commonly used by animal and plant cells in respiration include sugar , amino acids and fatty acids , and the most common oxidizing agent is molecular oxygen ...

  5. 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 ...

  6. Oxygen–hemoglobin dissociation curve - Wikipedia

    en.wikipedia.org/wiki/Oxygenhemoglobin...

    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 binding of the first oxygen molecule induces change in the shape of the ...

  7. Gas exchange - Wikipedia

    en.wikipedia.org/wiki/Gas_exchange

    The oxygen is held on the hemoglobin by four ferrous iron-containing heme groups per hemoglobin molecule. When all the heme groups carry one O 2 molecule each the blood is said to be "saturated" with oxygen, and no further increase in the partial pressure of oxygen will meaningfully increase the oxygen concentration of the blood.

  8. Hemoglobin A - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_A

    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 cell hemoglobin. [1] Hemoglobin is an oxygen-binding protein, found in erythrocytes , which transports oxygen from the lungs to the tissues. [ 2 ]

  9. Bohr effect - Wikipedia

    en.wikipedia.org/wiki/Bohr_effect

    Hemoglobin's oxygen binding affinity (see oxygen–haemoglobin dissociation curve) is inversely related both to acidity and to the concentration of carbon dioxide. [1] That is, the Bohr effect refers to the shift in the oxygen dissociation curve caused by changes in the concentration of carbon dioxide or the pH of the environment.