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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, alpha 2 - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin,_alpha_2

    15122 Ensembl ENSG00000188536 ENSMUSG00000069919 UniProt P69905 Q91VB8 RefSeq (mRNA) NM_000517 NM_008218 RefSeq (protein) NP_000508 NP_000508.1 NP_000549.1 NP_001077424 Location (UCSC) Chr 16: 0.17 – 0.17 Mb Chr 11: 32.23 – 32.23 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Hemoglobin, alpha 2 also known as HBA2 is a gene that in humans codes for the alpha globin chain of ...

  4. HBD - Wikipedia

    en.wikipedia.org/wiki/HBD

    n/a Ensembl ENSG00000223609 n/a UniProt P02042 n/a RefSeq (mRNA) NM_000519 n/a RefSeq (protein) NP_000510 n/a Location (UCSC) Chr 11: 5.23 – 5.24 Mb n/a PubMed search n/a Wikidata View/Edit Human Hemoglobin subunit delta is a protein that in humans is encoded by the HBD gene. Function The delta (HBD) and beta (HBB) genes are normally expressed in the adult: two alpha chains plus two beta ...

  5. 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 ]

  6. Haldane effect - Wikipedia

    en.wikipedia.org/wiki/Haldane_effect

    Thus, the Haldane effect describes the ability of hemoglobin to carry increased amounts of carbon dioxide (CO 2) in the deoxygenated state as opposed to the oxygenated state. Vice versa, it is true that a high concentration of CO 2 facilitates dissociation of oxyhemoglobin, though this is the result of two distinct processes (Bohr effect and ...

  7. Hemoglobin subunit alpha - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_subunit_alpha

    3039 15122 Ensembl ENSG00000206172 ENSMUSG00000069919 UniProt P69905 Q91VB8 RefSeq (mRNA) NM_000558 NM_008218 RefSeq (protein) NP_000508 NP_000508.1 NP_000549.1 NP_001077424 Location (UCSC) Chr 16: 0.18 – 0.18 Mb Chr 11: 32.23 – 32.23 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Hemoglobin subunit alpha, Hemoglobin, alpha 1, is a hemoglobin protein that in humans is encoded by ...

  8. Venous blood - Wikipedia

    en.wikipedia.org/wiki/Venous_blood

    The color of human blood ranges from bright red when oxygenated to a darker red when deoxygenated. [2] It owes its color to hemoglobin, to which oxygen binds. Deoxygenated blood is darker due to the difference in shape of the red blood cell when oxygen binds to haemoglobin in the blood cell (oxygenated) versus does not bind to it (deoxygenated).

  9. Hemoglobin subunit beta - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_subunit_beta

    In human, the HBB gene is located on chromosome 11 at position p15.5.. 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]

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