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Hemoglobin is the iron-containing oxygen-transport metalloprotein in the red blood cells of all vertebrates as well as the tissues of some invertebrates. Hemoglobin in the blood carries oxygen from the lungs or gills to the rest of the body (i.e. the tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power the functions of the organism in the process called metabolism. A healthy individual has “12 to 16” grams of haemoglobin in every 100 ml of blood.
In healthy men the protein makes up about 96% of the red blood cells’ dry content (by weight), and around 35% of the total content (including water). Hemoglobin has an oxygen-binding capacity of 1.34 mL O2 per gram which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood. The mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules.
Types of Hemoglobin
Hemoglobin variants are a part of the normal embryonic and fetal development. They may also be pathologic mutant forms of hemoglobin in a population, caused by variations in genetics. Some well-known hemoglobin variants, such as sickle-cell anemia, are responsible for diseases and are considered hemoglobinopathies. Other variants cause no detectable pathology, and are thus considered non-pathological variants.
In the embryo
- Gower 1 (ζ2ε2)
- Gower 2 (α2ε2)
- Hemoglobin Portland I (ζ2γ2)
- Hemoglobin Portland II (ζ2β2).
In the fetus:
- Hemoglobin F (α2γ2)
After birth
- Hemoglobin A (α2β2) (PDB: 1BZ0 ) – The most common with a normal amount over 95%
- Hemoglobin A2 (α2δ2) – δ chain synthesis begins late in the third trimester and, in adults, it has a normal range of 1.5–3.5%
- Hemoglobin F (α2γ2) – In adults Hemoglobin F is restricted to a limited population of red cells called F-cells. However, the level of Hb F can be elevated in persons with sickle-cell disease and beta-thalassemia.
- Hemoglobin D-Punjab – (α2βD2) – A variant form of hemoglobin.
- Hemoglobin H (β4) – A variant form of hemoglobin, formed by a tetramer of β chains, which may be present in variants of α thalassemia.
- Hemoglobin Barts (γ4) – A variant form of hemoglobin, formed by a tetramer of γ chains, which may be present in variants of α thalassemia.
- Hemoglobin S (α2βS2) – A variant form of hemoglobin found in people with sickle cell disease. There is a variation in the β-chain gene, causing a change in the properties of hemoglobin, which results in sickling of red blood cells.
- Hemoglobin C (α2βC2) – Another variant due to a variation in the β-chain gene. This variant causes a mild chronic hemolytic anemia.
- Hemoglobin E (α2βE2) – Another variant due to a variation in the β-chain gene. This variant causes a mild chronic hemolytic anemia.
- Hemoglobin AS – A heterozygous form causing sickle cell trait with one adult gene and one sickle cell disease gene
- Hemoglobin SC disease – A compound heterozygous form with one sickle gene and another encoding Hemoglobin C.
- Hemoglobin Hopkins-2 – A variant form of hemoglobin that is sometimes viewed in combination with Hemoglobin S to produce sickle cell disease.
Hemoglobin is involved in the transport of other gases: It carries some of the body’s respiratory carbon dioxide (about 20–25% of the total) as carbaminohemoglobin, in which CO2 is bound to the globin protein. The molecule also carries the important regulatory molecule nitric oxide bound to a globin protein thiol group, releasing it at the same time as oxygen.
How amount needed of Hemoglobin
Hemoglobin is also found outside red blood cells and their progenitor lines. Other cells that contain hemoglobin include the A9 dopaminergic neurons in the substantia nigra, macrophages, alveolar cells, lungs, retinal pigment epithelium, hepatocytes, mesangial cells in the kidney, endometrial cells, cervical cells and vaginal epithelial cells.In these tissues, hemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism.
Hemoglobin concentration measurement is among the most commonly performed blood tests, usually as part of a complete blood count. For example, it is typically tested before or after blood donation. Results are reported in g/L, g/dL or mol/L. 1 g/dL equals about 0.6206 mmol/L, although the latter units are not used as often due to uncertainty regarding the polymeric state of the molecule. This conversion factor, using the single globin unit molecular weight of 16,000 Da, is more common for hemoglobin concentration in blood. For MCHC (mean corpuscular hemoglobin concentration) the conversion factor 0.155, which uses the tetramer weight of 64,500 Da, is more common.Normal levels are:
- Men: 13.8 to 18.0 g/dL (138 to 180 g/L, or 8.56 to 11.17 mmol/L)
- Women: 12.1 to 15.1 g/dL (121 to 151 g/L, or 7.51 to 9.37 mmol/L)
- Children: 11 to 16 g/dL (110 to 160 g/L, or 6.83 to 9.93 mmol/L)
- Pregnant women: 11 to 14 g/dL (110 to 140 g/L, or 6.83 to 8.69 mmol/L) (9.5 to 15 usual value during pregnancy)
Normal values of hemoglobin in the 1st and 3rd trimesters of pregnant women must be at least 11 g/dL and at least 10.5 g/dL during the 2nd trimester.
Hemoglobin is an iron-rich protein present in red blood cells. This protein is responsible for carrying oxygen throughout the body.Its main function is to transport oxygen from the lungs to the body’s tissues, so that living cells can perform properly. Hemoglobin also helps carry carbon dioxide away from the cells and transport it back to the lungs.
10 Iron-Rich Fruits to Boost Haemoglobin Levels
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Fruit
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Amount per 100 g
|
|---|---|
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1. Sun-dried tomatoes
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9.1 mg
|
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2. Apricots, dehydrated
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6.3 mg
|
|
3. Raisins
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3 mg
|
|
4. Persimmons, raw
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2.5 mg
|
|
5. Mulberries, raw
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1.7 mg
|
|
6. Dates
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1 mg
|
|
7. Currants
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1 mg
|
|
8. Prunes
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0.9 mg
|
|
9. Pomegranate
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0.3 mg
|
|
10. Watermelon
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0.2 mg
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