hemoglobin

Also known as Hb, Hgb, haemoglobins, haemoglobin, hemoglobins

Hemoglobin (haemoglobin, Hb or Hgb) is a protein containing iron that facilitates the transportation of oxygen in red blood cells. Almost all vertebrates contain hemoglobin, with the sole exception of the fish family Channichthyidae. 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 12to 20grams of hemoglobin in every 100mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and a globulin.

AI overview

Hemoglobin is an iron-containing protein in red blood cells that transports oxygen from your lungs to the rest of your body, where it delivers that oxygen to power your cells. It's found in nearly all vertebrates and is essential for the aerobic respiration that keeps your metabolism running.

AI-generated from the Wikipedia summary — may contain errors.

Key facts

Heteropolypeptide.heteropolymer: Hemoglobin
Heteropolypeptide.polymer_type: heterotetramer, (αβ)2
Heteropolypeptide.protein_type: metalloprotein, chromoprotein, globulin
Heteropolypeptide.function: oxygen-transport
Heteropolypeptide.cofactors: heme (4)
Heteropolypeptide.image: 1GZX Haemoglobin.png
Heteropolypeptide.image_source: Structure of human hemoglobin. α and β globin subunits are in red and blue, respectively, and the iron-containing heme groups in green. From
Heteropolypeptide.SubunitCount: 3
Heteropolypeptide.subunit1: Hb-α1
Heteropolypeptide.gene1: HBA1
Heteropolypeptide.locus1: Chr. 16 p13.3
Heteropolypeptide.subunit2: Hb-α2
Heteropolypeptide.gene2: HBA2
Heteropolypeptide.locus2: Chr. 16 p13.3
Heteropolypeptide.subunit3: Hb-β
Heteropolypeptide.gene3: HBB
Heteropolypeptide.locus3: Chr. 11 p15.5
Heteropolypeptide.Formula: C2952 H 4664 O 832 N812 S8 Fe 4

via Wikipedia infobox

Research

283,484 papers

[Hemoglobin, from microorganisms to man: a single structural motif, multiple functions].ReviewComptes rendus biologies · 2002Wajcman H, Kiger LDOI: 10.1016/s1631-0691(02)01537-8
[Role of alpha-hemoglobin molecular chaperone in the hemoglobin formation and clinical expression of some hemoglobinopathies].ReviewTransfusion clinique et biologique : journal de la Societe francaise de transfusion sanguine · 2015Vasseur C, Baudin-Creuza VDOI: 10.1016/j.tracli.2015.01.002
HUMAN HAEMOGLOBINS.ReviewJournal of medical genetics · 1965HUEHNS ER, SHOOTER EMDOI: 10.1136/jmg.2.1.48
Hemosomegenesis and hemoglobin biosynthesis in vertebrates.ReviewComparative biochemistry and physiology. Comparative physiology · 1992Brunner Júnior A, de Rizzo E, Morena DD et al.DOI: 10.1016/0300-9629(92)90718-6
Hemoglobin S-C disease.The American journal of roentgenology, radium therapy, and nuclear medicine · 1962BECKER JA
[Fetal hemoglobin].Vie medicale (Paris, France : 1920) · 1954DUGAS M
[Red cell substitutes: perfluorocarbon emulsions and hemoglobin solutions].ReviewAnnales francaises d'anesthesie et de reanimation · 1999Rémy B, Deby-Dupont G, D'Ans V et al.DOI: 10.1016/s0750-7658(99)80072-0
[Hemoglobin SD disease].Monatsschrift Kinderheilkunde : Organ der Deutschen Gesellschaft fur Kinderheilkunde · 1993Laws HJ, Dickerhoff R, Mayer J et al.

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Wikidata facts

Image: Redbloodcells.jpg

Show 2 more facts

chemical formula: C₂₉₅₂H₄₆₆₄O₈₁₂₅S₈Fe₄₃₂₁
Commons category: Hemoglobin

Sources (4)

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~51 min read

Article

31 sections

Contents

Research history
Genetics
Evolution
Evolution of vertebrate hemoglobin
Fish
Birds
Mammals
Synthesis
Structure of heme
Oxygen saturation
Oxyhemoglobin
Deoxygenated hemoglobin
Cooperativity
Binding of ligands other than oxygen
Competitive
Allosteric
Types of hemoglobin in humans
Degradation in vertebrate animals
Diseases related to hemoglobin
Diagnostic uses
Athletic tracking and self-tracking uses
Analogues in non-vertebrate organisms
Other oxygen-binding proteins
Presence in nonerythroid cells
In history and art
See also
References
Notes
Sources
Further reading
External links

In mammals, hemoglobin makes up about 96% of a red blood cell's dry weight (excluding water), and around 35% of the total weight (including water). Hemoglobin has an oxygen-binding capacity of 1.34mL of O2 per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. The mammalian hemoglobin molecule can bind and transport up to four oxygen molecules.