513:. Alpha-thalassemia is a genetic blood disorder and one of the most common hemoglobin-related diseases, affecting the production of α subunits from hemoglobin. Depending on how many genes coding for the α subunit are impacted (between one and four), patients with this disease can have reduced to no production of the α subunit of the hemoglobin. As a consequence, less hemoglobin is available and this affects oxygen supply to the tissues. Hemoglobin Barts syndrome manifests when all four genes coding for α subunit are deleted. This is often fatal for the fetus carrying the disorder, as in the absence of α subunits, a form of hemoglobin with four γ subunits, hemoglobin Barts, is produced. This form of hemoglobin isn't fit for oxygen exchange precisely due to its very high affinity for oxygen. While hemoglobin Barts is very efficient at binding oxygen, it doesn't release oxygen to the organs and tissues. The disease is fatal for the fetus or newborn unless early diagnosis and intervention is carried out during pregnancy, and the child will be dependent on lifelong blood transfusions.
617:
other blood-related diseases. In this condition, the genes coding for the γ subunit (HBG1 and HBG2) are not suppressed shortly before birth. This can happen when a mutation occurs in the promoter region of HBG1 and HBG2, preventing the binding of BCL11A and ZBTB7A proteins. These proteins would normally bind and suppress the production of γ subunits and as they can't bind due to the mutation, γ subunits continue to be produced. There are two types of patients with HPFH: either with one normal copy of the gene and one disease form or with two disease copies. Whereas normal adults have less than 1% of hemoglobin F, patients with only one disease gene have 5-30%. Patients with two disease copies can have hemoglobin F in up to 100% of red blood cells. As other diseases such as sickle cell disease could also cause a higher level of hemoglobin F to be present, it can sometimes be misdiagnosed.
461:, which has 3 variants depending on the types of subunits it contains. The production of hemoglobin F starts from week 6, but it's only from 3 months onwards that it becomes the main type found in fetal red blood cells. The switch to produce adult forms of hemoglobin (essentially hemoglobin A) starts at around 40 weeks of gestation, which is close to the expected time of birth. At birth, hemoglobin F accounts for 50-95% of the infant's hemoglobin and at around 6 months after birth, hemoglobin A becomes the predominant type. By the time the baby is one year old, the proportions of different types of hemoglobin are expected to approximate the adult levels, with hemoglobin F reduced to very low levels. The small proportion of red blood cells containing hemoglobin F are called F-cells, which also contain other types of hemoglobin.
565:
hemoglobin F being present and its tendency to be produced only in a subset of cells rather than evenly distributed amongst all red blood cells. In fact, there is a positive correlation between the levels of hemoglobin F and number of F-cells, with patients with higher percentages of hemoglobin F also having a higher proportion of F-cells. Despite the correlations between hemoglobin F levels and F-cell numbers, usually they are determined by direct measurements. While the amount of hemoglobin F is calculated using cell lysates, which are fluids with contents of cells that were broken open, F-cell numbers are done by counting intact red blood cells.
687:, which is a hallmark of the disease. If fetal hemoglobin remains relatively high after birth, the number of painful episodes decreases in patients with sickle-cell disease and they have a better prognosis. Fetal hemoglobin's role in reducing disease severity comes from its ability to disrupt the formation of hemoglobin S chains within red blood cells. Interestingly, while higher levels of hemoglobin F were associated with improvement of some symptoms, including the frequency of painful episodes, leg ulcers and the general severity of the disease, it had no correlation to others. A few examples are
710:
and myeloid leukemia in children, where higher concentrations of hemoglobin F were associated with a worse outcome, including a higher risk of relapse or death. Other cancer types where higher hemoglobin F levels have been observed are transitional cell cancer, colorectal carcinoma and various types of blastomas. In fact, in several types of blastomas, including neuroblastoma and retinoblastoma (affecting the nerve cells and the eyes, respectively), F-cells were found in newly formed blood vessels and spaces in between tumour cells. Clusters of F-cells were also present in the
552:). Secondly, the mother's bloodstream is richer in oxygen than that of the fetus, so oxygen naturally flows towards the fetal circulation by diffusion. The final factor is related to the effects of pH on maternal and fetal hemoglobin. As the maternal blood acquires more carbon dioxide, it becomes more acidic and this favors the release of oxygen by the maternal hemoglobin. At the same time, the decrease in carbon dioxide in fetal blood makes it more alkaline and favors the uptake of oxygen. This is called the Bohr effect or
53:
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of F-cells in pregnant women, which was observed between the 23rd to 31st week of gestation. However, as to the reason of the increase in hemoglobin F levels in pregnant women, there doesn't seem to be conclusive evidence. While an early study suggested that maternal red blood cells switch on hemoglobin F production during pregnancy, more recent literature suggested that the increase in haemoglobin F could be, at least in part, due to fetal red blood cells being transferred to the maternal circulation.
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it becomes a competition between fetal and maternal hemoglobin F which have similar affinities for oxygen. As a result, women with hemoglobin F as >70% of total hemoglobin are much more likely to have fetuses that are small for their gestational age compared women with <70% hemoglobin F (at a rate of 100% compared to 8%, respectively).
580:. Additionally, some acquired conditions can also have higher F-cell numbers, such as acute erythropoietic stress (response to poor oxygenation which includes very rapid synthesis of new red blood cells) and pregnancy. F-cells have similar mass of haemoglobin per cell compared to red blood cells without haemoglobin F, which is measured
691:, stroke and systemic blood pressure. As hemoglobin F are only produced by some red blood cells, in different quantities, only a subpopulation of cells are protected against sickling. It could be that the symptoms that high hemoglobin F doesn't prevent are quite sensitive to the rupture of the sickled non-F cells.
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Delta beta-thalassemia is a rare genetic blood disorder in which the production of both δ and β subunits are reduced or absent. In these cases, the production of the γ subunit increases to compensate for the loss of δ and β subunits, resulting in a higher amount of hemoglobin F present in the blood.
601:
Presence of high levels of hemoglobin F in pregnant women can impact the growth of the fetus, as fetal red blood cells struggle to compete for the oxygen from the mother's circulation. This is because instead of competing with hemoglobin A, which has a weaker association to oxygen than hemoglobin F,
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There is a significant increase in hemoglobin F levels during early pregnancy. However, it's not clear whether these levels are stable or decrease as the pregnancy goes on, as different sources reported different results. The increase in hemoglobin F then induces a 3 to 7 fold increase in the number
405:
BCL11A and ZBTB7A are major repressor proteins of hemoglobin F production, by binding to the gene coding for the γ subunit at their promoter region. This happens naturally as the newborn baby starts to switch from producing hemoglobin F to producing hemoglobin A. Some genetic diseases can take place
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There have been some studies evaluating the possibility of using hemoglobin F as an indicator of the prognosis for cancer. It has been suggested that elevated concentrations of haemoglobin F can be found in main kinds of solid tumours and blood cancers. Examples include acute lymphoblastic leukemia
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The discovery that hemoglobin F alleviated the symptoms of sickle cell disease occurred in 1948. Janet Watson observed that red blood cells from infants with the disease took longer to sickle and did not deform as much compared to their mother's cells, which carried the disease trait. Later, it was
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The four hemes, which are the oxygen-binding parts of hemoglobin, are similar between hemoglobin F and other types of hemoglobin, including hemoglobin A. Thus, the key feature that allows hemoglobin F to bind more strongly to oxygen is by having γ subunits (instead of β, for example). In fact, some
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This is a rare benign genetic disease where production of hemoglobin F persists after twelve months of life and into the adulthood. As a result, hemoglobin F is present in a higher number of adult red blood cells than normal. It doesn't present symptoms and is usually discovered when screening for
537:
During pregnancy, the mother's circulatory system delivers oxygen and nutrients to the fetus and carries away nutrient-depleted blood enriched with carbon dioxide. The maternal and fetal blood circulations are separate and the exchange of molecules occurs through the placenta, in a region called
714:
of some of these patients. Interestingly, hemoglobin F is not directly produced by tumour cells, but seems to be induced by the biological environment of the cancer in nearby blood cells. A reason suggested for this increase in hemoglobin F is that it may favor cancer growth by providing better
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F-cells are the subpopulation of red blood cells that contain hemoglobin F, in amongst other types of hemoglobin. While common in fetuses, in normal adults, only around 3-7% of red blood cells contain hemoglobin F. The low percentage of F-cells in adults owes to two factors: very low levels of
497:
and it enhances hemoglobin's ability to release oxygen. 2,3-BPG interacts much more with hemoglobin A than hemoglobin F. This is because the adult β subunit has more positive charges than the fetal γ subunit, which attract the negative charges from 2,3-BPG. Due to the preference of 2,3-BPG for
521:
To quantify how strongly a certain type of hemoglobin binds to oxygen (or its affinity for oxygen), a parameter called P50 is often used. In a given situation, P50 can be understood as the partial pressure of oxygen at which Hb is 50% saturated. For example, Hemoglobin F has a lower P50 than
522:
hemoglobin A. This means that if we have the same amount of hemoglobin F and hemoglobin A in the blood and add oxygen to it, half of hemoglobin F will bind to oxygen before half of hemoglobin A manages to do so. Therefore, a lower P50 means stronger binding or higher affinity for oxygen.
369:. The protein that they produce is identical, but they differ in gene regulatory regions that determine when or how much of the protein is produced. This leads to HBA1 and HBA2 contributing 40% and 60%, respectively, of the total α subunits produced. As a consequence, mutations on the
545:
Focusing on oxygen exchange, there are three important aspects that allow oxygen to pass from the maternal circulation into the fetal circulation. Firstly, the presence of hemoglobin F in the fetus allows a stronger binding to oxygen than maternal hemoglobin (see
1599:"Fetal hemoglobin-containing cells have the same mean corpuscular hemoglobin as cells without fetal hemoglobin: a reciprocal relationship between gamma- and beta-globin gene expression in normal subjects and in those with high fetal hemoglobin production"
626:
Normally, people have two sets of genes for producing δ and β subunits. People with only one set of working genes don't get any symptoms and in the rarely reported cases where both sets of genes are affected, the patients only experienced mild symptoms.
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noted that patients with sickle cell trait as well as hereditary persistence of hemoglobin F (HPFH) didn't have symptoms. Additionally, in sickle cell patients, F-cells were found to be more long living than non-F cells as they contain hemoglobin F.
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In the newborn, levels of hemoglobin F gradually decrease and reach adult levels (less than 1% of total hemoglobin) usually within the first year, as adult forms of hemoglobin begin to be produced. Diseases such as
1737:
Boyer SH, Belding TK, Margolte L, Noyes AN, Burke PJ, Bell WR (September 1975). "Variations in the frequency of fetal hemoglobin-bearing erythrocytes (F-cells) in well adults, pregnant women, and adult leukemics".
677:-shaped. These defective red blood cells have a much shorter life span than normal red blood cells (10–20 days compared to up to 120 days). They also have a greater tendency to clump together and block small
715:
oxygen supply to the developing cancerous cells. In adults, increased hemoglobin F production is thought to be caused by factors leading to the activation of the gene coding for the γ subunit, such as
2639:
1681:
Yamada T, Morikawa M, Yamada T, Nishida R, Takeda M, Kawaguchi S, Minakami H (January 2013). "Changes in hemoglobin F levels in pregnant women unaffected by clinical fetomaternal hemorrhage".
1063:
Martyn GE, Wienert B, Yang L, Shah M, Norton LJ, Burdach J, et al. (April 2018). "Natural regulatory mutations elevate the fetal globin gene via disruption of BCL11A or ZBTB7A binding".
2196:
Ma Q, Wyszynski DF, Farrell JJ, Kutlar A, Farrer LA, Baldwin CT, Steinberg MH (December 2007). "Fetal hemoglobin in sickle cell anemia: genetic determinants of response to hydroxyurea".
2336:
Rautonen J, Siimes MA (July 1990). "Initial blood fetal hemoglobin concentration is elevated and is associated with prognosis in children with acute lymphoid or myeloid leukemia".
556:, which also happens in the air exchange in the lungs. All of these three factors are present simultaneously and cooperate to improve the fetus’ access to oxygen from the mother.
278:, allowing it to bind (or attach to) oxygen more strongly; this in turn enables the developing fetus to retrieve oxygen from the mother's bloodstream, which occurs through the
697:
is a chemical that promotes the production of fetal hemoglobin and reduces the premature rupturing of red blood cells. Combination therapy with hydroxyurea and recombinant
3347:
1458:
Italia KY, Colah R, Mohanty D (December 2007). "Evaluation of F cells in sickle cell disorders by flow cytometry -- comparison with the
Kleihauer-Betke's slide method".
701:— rather than treatment with hydroxyurea alone — has been shown to further elevate hemoglobin F levels and to promote the development of HbF-containing F-cells.
3382:
2241:"Effect of hydroxyurea on the frequency of painful crises in sickle cell anemia. Investigators of the Multicenter Study of Hydroxyurea in Sickle Cell Anemia"
2595:
1808:
Murji A, Sobel ML, Hasan L, McLeod A, Waye JS, Sermer M, Berger H (February 2012). "Pregnancy outcomes in women with elevated levels of fetal hemoglobin".
2615:
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Wolk M, Newland AC, De La Salle B (1999). "Refinement of plasma fetal hemoglobin (HbF) measurements, as related to whole blood HbF, in cancer patients".
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Due to the correlation between the amount of hemoglobin F and F-cells, F-cell numbers are higher in some inherited hemoglobin disorders, including
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For reference, the P50 of fetal hemoglobin is roughly 19 mmHg (a measure of pressure), whereas adult hemoglobin is approximately 26.8 mmHg (see
2666:
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Sripichai O, Fucharoen S (December 2016). "Fetal hemoglobin regulation in β-thalassemia: heterogeneity, modifiers and therapeutic approaches".
1973:
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of hemoglobin before and after birth, also showing the cells types and organs where different subunits are being produced over time (data on
2149:"Fetal hemoglobin in sickle cell anemia: molecular characterization of the unusually high fetal hemoglobin phenotype in African Americans"
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1878:
Thein SL, Craig JE (1998). "Genetics of Hb F/F cell variance in adults and heterocellular hereditary persistence of fetal hemoglobin".
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group with an iron element which is key in allowing the binding and unbinding of oxygen. As such, hemoglobin F can adopt two states:
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When fetal hemoglobin production is switched off after birth, normal children begin producing adult hemoglobin (HbA). Children with
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naturally existing molecules in our body can bind to hemoglobin and change its binding affinity for oxygen. One of the molecules is
3367:
464:
In healthy adults, the composition of hemoglobin is hemoglobin A (~97%), hemoglobin A2 (2.2 - 3.5%) and hemoglobin F (<1%).
1333:
Awasthi V, Goins E, Phillips W (2006). "Chapter 43 – Liposome-encapsulated hemoglobin: history, preparation and evaluation".
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is an abnormal form of hemoglobin produced in hemoglobin Barts syndrome or alpha-thalassemia major, the most severe form of
467:
Certain genetic abnormalities can cause the switch to adult hemoglobin synthesis to fail, resulting in a condition known as
2620:
2640:
Chapter 26 Fetal
Hemoglobin Induction; Management of Sickle-Cell Disease 4th Edition 2002 (NIH Publication No. 02-2117)
2634:
1765:
Dana M, Fibach E (March 2018). "Fetal
Hemoglobin in the Maternal Circulation - Contribution of Fetal Red Blood Cells".
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can cause hemoglobin F to still be produced after the switch to hemoglobin A should have occurred, which is called
342:
subunits, whereas hemoglobin A (97% of total hemoglobin in adults) is composed of two α and two β (beta) subunits.
334:(without oxygen). As hemoglobin F has 4 heme groups, it can bind to up to four oxygen molecules. It is composed of
1502:
1108:"Evaluation of Alpha-Thalassemia Mutations in Cases with Hypochromic Microcytic Anemia: The İstanbul Perspective"
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1507:"F-cells in the adult: normal values and levels in individuals with hereditary and acquired elevations of Hb F"
1041:
2812:
2793:
2756:
494:
1358:
Yacov R, Derek K, Namasivayam A (2017). "Chapter 10 – Blood gases: technical aspects and interpretation".
302:, increasing the production of hemoglobin F has been used as a treatment to relieve some of the symptoms.
841:
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1216:
683:
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350:
346:
52:
2282:"Augmentation by erythropoietin of the fetal-hemoglobin response to hydroxyurea in sickle cell disease"
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Ibrahim M, Qari MH, Sait W, Abulela M (2009). "Pattern of HB F level rise during normal pregnancies".
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2077:. The Johns Hopkins University, The Johns Hopkins Hospital, and Johns Hopkins Health System. 2020
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1548:"Stress-associated erythropoiesis initiation is regulated by type 1 conventional dendritic cells"
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Akinsheye I, Alsultan A, Solovieff N, Ngo D, Baldwin CT, Sebastiani P, et al. (July 2011).
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Akinsheye I, Solovieff N, Ngo D, Malek A, Sebastiani P, Steinberg MH, Chui DH (February 2012).
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1217:"Comparing the molecular structure differences between HbF and HbA that affect BPG binding"
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During the first 3 months of pregnancy, the main form of hemoglobin in the embryo/fetus is
3327:
3182:
1045:
442:
319:
2435:"Development of fetal haemoglobin-blood cells (F cells) within colorectal tumour tissues"
2239:
Charache S, Terrin ML, Moore RD, Dover GJ, Barton FB, Eckert SV, et al. (May 1995).
2487:"Foetal haemoglobin-blood cells (F-cells) as a feature of embryonic tumours (blastomas)"
2045:
1106:
Karakaş Z, Koç B, Temurhan S, Elgün T, Karaman S, Asker G, et al. (December 2015).
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Lanzkron S, Strouse JJ, Wilson R, Beach MC, Haywood C, Park H, et al. (June 2008).
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weeks of pregnancy and the levels remain high after birth until the baby is roughly 2–4
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Rodgers GP, Dover GJ, Uyesaka N, Noguchi CT, Schechter AN, Nienhuis AW (January 1993).
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1995:
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2098:"Vaso-occlusion in sickle cell disease: pathophysiology and novel targeted therapies"
1471:
1383:
Metcalfe J, Bartels H, Moll W (October 1967). "Gas exchange in the pregnant uterus".
915:"Systematic review: Hydroxyurea for the treatment of adults with sickle cell disease"
315:
298:, can delay this process, and cause hemoglobin F levels to be higher than normal. In
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Increasing the body's production of fetal hemoglobin is used as a strategy to treat
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gene. There are also two similar copies of the gene coding for the γ subunit,
3317:
3275:
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2701:
1964:
Wahed A, Dasgupta A (2015). "Chapter 4 – Hemoglobinopathes and
Thalassemias".
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due to mutations to genes coding for components of hemoglobin F. Mutations to
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331:
327:
275:
681:, preventing blood supply to tissues and organs. This leads to the so-called
3258:
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2450:
1915:"Blessing in disguise; a case of Hereditary Persistence of Fetal Hemoglobin"
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1950:
1829:
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1583:
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hemoglobin A, hemoglobin F binds to oxygen with more affinity, in average.
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1404:
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719:(which can activate normally silent genes and is a hallmark of cancer).
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402:
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2554:
2538:"DNA demethylation and invasive cancer: implications for therapeutics"
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subunits are in red and yellow, respectively, and the iron-containing
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240:
102:
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gene are expected to have a stronger effect than mutations on the
247:
1683:
Clinica
Chimica Acta; International Journal of Clinical Chemistry
820:
Wang Y, Zhao S (2010). "Chapter 2: Placental Blood
Circulation".
2853:
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1190:
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Even higher oxygen affinity – hemoglobin Barts (four γ subunits)
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which is located in between maternal and fetal blood vessels.
385:, but the protein produced is slightly different, just in one
262:
to organs and tissues in the fetus. It is produced at around 6
2384:"Fetal haemopoiesis marking low-grade urinary bladder cancer"
1424:
Continuing
Education in Anaesthesia, Critical Care & Pain
1163:
Continuing
Education in Anaesthesia, Critical Care & Pain
2616:
Hemoglobin structure and function (archived
February 3, 2002
1919:
Journal of Community Hospital Internal Medicine Perspectives
768:"Hemoglobin research and the origins of molecular medicine"
258:, and is involved in transporting oxygen from the mother's
1546:
Kim TS, Hanak M, Trampont PC, Braciale TJ (October 2015).
2600:
1913:
Shaukat I, Pudal A, Yassin S, Höti N, Mustafa S (2018).
483:
Oxygen-hemoglobin dissociation curves in fetus and adult
1853:"FETAL HEMOGLOBIN QUANTITATIVE TRAIT LOCUS 1; HBFQTL1"
665:
begin producing a defective form of hemoglobin called
547:
1810:
The Journal of Maternal-Fetal & Neonatal Medicine
968:. Hagerstwon, MD: Lippincott Williams & Wilkins.
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Fetal hemoglobin (doc file; archived March 30 2003)
2621:
Hemoglobin F fact sheet (archived October 29, 2009)
109:
98:
84:
32:
274:F has a different composition than adult forms of
1420:"Placental structure, function and drug transfer"
606:Hereditary persistence of fetal hemoglobin (HPFH)
1284:"Classification of the disorders of hemoglobin"
1460:International Journal of Laboratory Hematology
908:
906:
2660:
2536:Cheishvili D, Boureau L, Szyf M (June 2015).
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8:
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1989:
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79:, by authors Soman, J. and Olson J.S.
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612:Hereditary persistence of fetal hemoglobin
578:hereditary persistence of fetal hemoglobin
469:hereditary persistence of fetal hemoglobin
428:hereditary persistence of fetal hemoglobin
51:
3348:disorders of globin and globulin proteins
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2433:Wolk M, Martin JE, Reinus C (June 2006).
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2011:
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418:and mutations to the promoter regions of
57:Structure of fetal hemoglobin (HbF). The
27:Oxygen carrier protein in the human fetus
2096:Manwani D, Frenette PS (December 2013).
1996:"Fetal hemoglobin in sickle cell anemia"
931:10.7326/0003-4819-148-12-200806170-00221
2601:American Sickle Cell Anemia Association
728:
453:) Figure last adapted by user Leonid 2.
345:In humans, the α subunit is encoded on
824:. Morgan & Claypool Life Sciences.
669:instead, which form chains that cause
653:Sickle-cell disease § Hydroxyurea
29:
1552:The Journal of Clinical Investigation
1243:"Gene test review. Alpha-thalassemia"
995:Blood Cells, Molecules & Diseases
843:Dacie and Lewis Practical Haematology
310:Hemoglobin F, like adult hemoglobin (
7:
1282:Forget BG, Bunn HF (February 2013).
1241:Galanello R, Cao A (February 2011).
989:Farashi S, Harteveld CL (May 2018).
705:Hemoglobin F as a marker for cancers
673:to change their shape from round to
3383:Embryology of cardiovascular system
2286:The New England Journal of Medicine
2245:The New England Journal of Medicine
1360:Assisted Ventilation of the Neonate
393:codes for the protein form with an
322:or chains. Each subunit contains a
2631:Hydroxyurea in sickle-cell disease
1505:, Lim G, Nute PE (November 1975).
991:"Molecular basis of α-thalassemia"
25:
2050:U.S. National Library of Medicine
1740:The Johns Hopkins Medical Journal
1597:Dover GJ, Boyer SH (April 1987).
588:Conditions with high hemoglobin F
549:Factors affecting oxygen affinity
495:2,3-bisphosphoglycerate (2,3-BPG)
488:Factors affecting oxygen affinity
294:, which affect components of the
1472:10.1111/j.1365-2257.2006.00884.x
1418:Griffiths S, Campbell J (2015).
822:Vascular Biology of the Placenta
635:Treatment of sickle-cell disease
517:Quantification of oxygen binding
349:and the γ subunit is encoded on
2633:(archived December 28, 2014 at
2542:British Journal of Pharmacology
2382:Wolk M, Martin JE (July 2012).
2153:American Journal of Hematology
1112:Turkish Journal of Haematology
766:Schechter AN (November 2008).
1:
2606:SCDAA: Break The Sickle Cycle
2596:Transport across the placenta
2439:Journal of Clinical Pathology
1932:10.1080/20009666.2018.1536241
1851:Hemosh A (9 September 2014).
1779:10.1080/03630269.2018.1466712
1397:10.1152/physrev.1967.47.4.782
881:10.1080/17474086.2016.1255142
745:(second ed.). Elsevier.
357:that code for the α subunit,
353:. There are two very similar
121:
2198:The Pharmacogenomics Journal
2115:10.1182/blood-2013-05-498311
2013:10.1182/blood-2011-03-325258
1822:10.3109/14767058.2011.564241
1362:(sixth ed.). Elsevier.
1260:10.1097/GIM.0b013e3181fcb468
785:10.1182/blood-2008-04-078188
2299:10.1056/NEJM199301143280201
2258:10.1056/NEJM199505183322001
1301:10.1101/cshperspect.a011684
1159:"Physiology of haemoglobin"
919:Annals of Internal Medicine
869:Expert Review of Hematology
846:(12th ed.). Elsevier.
533:Oxygen exchange in the womb
3399:
1966:Hematology and Coagulation
1859:. Johns Hopkins University
1157:Thomas C, Lumb AB (2012).
1008:10.1016/j.bcmd.2017.09.004
742:Encyclopedia of Immunology
650:
609:
3343:
2491:British Journal of Cancer
2388:British Journal of Cancer
1892:10.3109/03630269809071538
1695:10.1016/j.cca.2012.10.002
1652:10.3109/03630260903332981
1077:10.1038/s41588-018-0085-0
397:at position 136, whereas
120:
50:
37:
1437:10.1093/bjaceaccp/mku013
1176:10.1093/bjaceaccp/mks025
2451:10.1136/jcp.2005.029934
451:Br. Med. Bull. 32, 282.
3368:Protein heteropolymers
2504:10.1038/sj.bjc.6603867
2210:10.1038/sj.tpj.6500433
2075:Johns Hopkins Medicine
648:
621:Delta beta-thalassemia
484:
454:
330:(bound to oxygen) and
306:Structure and genetics
282:found in the mother's
270:months old. Hemoglobin
69:groups in green. From
2071:"Sickle Cell Disease"
2046:"Sickle cell disease"
1385:Physiological Reviews
1125:10.4274/tjh.2014.0204
684:vaso-occlusive crisis
642:
630:Clinical significance
582:mean cell haemoglobin
482:
441:
2611:Hemoglobin synthesis
2401:10.1038/bjc.2012.268
1503:Stamatoyannopoulos G
1247:Genetics in Medicine
962:Costanzo LS (2007).
459:embryonic hemoglobin
254:F is found in fetal
3204:Glycated hemoglobin
3174:Carbaminohemoglobin
663:sickle-cell disease
645:sickle-cell disease
2591:Hemoglobinopathies
2350:10.1007/BF01739428
1337:. Academic press.
1194:. Academic press.
1192:Human Biochemistry
1044:2020-07-31 at the
649:
574:sickle cell anemia
540:intervillous space
485:
455:
300:sickle cell anemia
218:foetal haemoglobin
131:Chromosomal locus
3355:
3354:
3306:
3305:
3302:
3301:
3238:
3237:
3169:Carboxyhemoglobin
3157:
3156:
3050:
3049:
2864:
2863:
2555:10.1111/bph.12885
2165:10.1002/ajh.22221
2052:. NIH. 2020-03-15
1975:978-0-12-800241-4
1369:978-0-323-39006-4
1344:978-0-12-759760-7
1335:Blood Substitutes
1201:978-0-12-383864-3
875:(12): 1129–1137.
853:978-0-7020-6696-2
752:978-0-12-226765-9
717:DNA demethylation
527:Blood gas tension
511:alpha-thalassemia
475:Binding to oxygen
416:alpha-thalassemia
292:beta thalassemias
211:
210:
207:
206:
18:Fetal haemoglobin
16:(Redirected from
3390:
3247:
2886:
2875:
2714:
2707:
2698:
2669:
2662:
2655:
2646:
2578:
2577:
2567:
2557:
2533:
2527:
2526:
2516:
2506:
2482:
2473:
2472:
2462:
2430:
2424:
2423:
2413:
2403:
2379:
2370:
2369:
2333:
2327:
2326:
2323:Journal of Tumor
2318:
2312:
2311:
2301:
2277:
2271:
2270:
2260:
2236:
2230:
2229:
2193:
2187:
2186:
2176:
2144:
2138:
2137:
2127:
2117:
2093:
2087:
2086:
2084:
2082:
2067:
2061:
2060:
2058:
2057:
2042:
2036:
2035:
2025:
2015:
1991:
1980:
1979:
1961:
1955:
1954:
1944:
1934:
1910:
1904:
1903:
1875:
1869:
1868:
1866:
1864:
1848:
1842:
1841:
1805:
1799:
1798:
1762:
1756:
1755:
1734:
1725:
1724:
1706:
1678:
1672:
1671:
1635:
1629:
1628:
1618:
1594:
1588:
1587:
1577:
1567:
1565:10.1172/JCI81919
1543:
1537:
1536:
1526:
1498:
1492:
1491:
1455:
1442:
1441:
1439:
1415:
1409:
1408:
1380:
1374:
1373:
1355:
1349:
1348:
1330:
1324:
1323:
1313:
1303:
1279:
1273:
1272:
1262:
1238:
1232:
1231:
1229:
1227:
1215:Sears D (2016).
1212:
1206:
1205:
1187:
1181:
1180:
1178:
1154:
1148:
1147:
1137:
1127:
1103:
1097:
1096:
1060:
1049:
1037:
1031:
1030:
1020:
1010:
986:
980:
979:
959:
953:
952:
942:
910:
901:
900:
864:
858:
857:
837:
826:
825:
817:
808:
807:
797:
787:
763:
757:
756:
739:Linch D (1998).
736:
593:During pregnancy
570:beta-thalassemia
507:Hemoglobin Barts
414:genes can cause
296:adult hemoglobin
273:
269:
265:
253:
214:Fetal hemoglobin
122:
78:
55:
33:Fetal hemoglobin
30:
21:
3398:
3397:
3393:
3392:
3391:
3389:
3388:
3387:
3358:
3357:
3356:
3351:
3339:
3328:Cytochrome P450
3298:
3280:
3234:
3213:
3192:
3183:Deoxyhemoglobin
3153:
3149:
3145:
3135:
3131:
3121:
3117:
3107:
3103:
3093:
3089:
3079:
3069:
3046:
3042:
3038:
3028:
3024:
3019:
3011:
3007:
2990:
2986:
2982:
2972:
2968:
2951:
2947:
2943:
2938:HbE Portland II
2933:
2929:
2919:
2915:
2905:
2901:
2880:
2860:
2787:
2718:Alpha locus on
2687:
2673:
2587:
2582:
2581:
2548:(11): 2705–15.
2535:
2534:
2530:
2484:
2483:
2476:
2432:
2431:
2427:
2381:
2380:
2373:
2335:
2334:
2330:
2320:
2319:
2315:
2279:
2278:
2274:
2251:(20): 1317–22.
2238:
2237:
2233:
2195:
2194:
2190:
2146:
2145:
2141:
2095:
2094:
2090:
2080:
2078:
2069:
2068:
2064:
2055:
2053:
2044:
2043:
2039:
1993:
1992:
1983:
1976:
1963:
1962:
1958:
1912:
1911:
1907:
1886:(5–6): 401–14.
1877:
1876:
1872:
1862:
1860:
1850:
1849:
1845:
1807:
1806:
1802:
1764:
1763:
1759:
1736:
1735:
1728:
1680:
1679:
1675:
1637:
1636:
1632:
1596:
1595:
1591:
1558:(10): 3965–80.
1545:
1544:
1540:
1500:
1499:
1495:
1457:
1456:
1445:
1417:
1416:
1412:
1382:
1381:
1377:
1370:
1357:
1356:
1352:
1345:
1332:
1331:
1327:
1281:
1280:
1276:
1240:
1239:
1235:
1225:
1223:
1214:
1213:
1209:
1202:
1189:
1188:
1184:
1156:
1155:
1151:
1105:
1104:
1100:
1065:Nature Genetics
1062:
1061:
1052:
1046:Wayback Machine
1038:
1034:
988:
987:
983:
976:
961:
960:
956:
912:
911:
904:
866:
865:
861:
854:
840:Wild B (2017).
839:
838:
829:
819:
818:
811:
778:(10): 3927–38.
765:
764:
760:
753:
738:
737:
730:
725:
707:
671:red blood cells
655:
637:
632:
623:
614:
608:
595:
590:
562:
535:
519:
504:
490:
477:
443:Gene expression
436:
332:deoxyhemoglobin
308:
271:
267:
263:
256:red blood cells
251:
244:carrier protein
237:
233:
80:
70:
45:
41:
28:
23:
22:
15:
12:
11:
5:
3396:
3394:
3386:
3385:
3380:
3375:
3370:
3360:
3359:
3353:
3352:
3344:
3341:
3340:
3338:
3337:
3332:
3331:
3330:
3325:
3314:
3312:
3308:
3307:
3304:
3303:
3300:
3299:
3297:
3296:
3290:
3288:
3282:
3281:
3279:
3278:
3273:
3268:
3267:
3266:
3255:
3253:
3244:
3240:
3239:
3236:
3235:
3233:
3232:
3230:Erythrocruorin
3227:
3221:
3219:
3215:
3214:
3212:
3211:
3206:
3200:
3198:
3194:
3193:
3191:
3190:
3188:Sulfhemoglobin
3185:
3176:
3171:
3165:
3163:
3159:
3158:
3155:
3154:
3152:
3151:
3147:
3143:
3137:
3133:
3129:
3123:
3119:
3115:
3109:
3105:
3101:
3095:
3091:
3087:
3081:
3077:
3071:
3067:
3060:
3058:
3052:
3051:
3048:
3047:
3045:
3044:
3040:
3036:
3030:
3026:
3022:
3017:
3013:
3009:
3005:
2998:
2996:
2992:
2991:
2989:
2988:
2984:
2980:
2974:
2970:
2966:
2959:
2957:
2953:
2952:
2950:
2949:
2945:
2941:
2935:
2931:
2927:
2924:HbE Portland I
2921:
2917:
2913:
2907:
2903:
2899:
2892:
2890:
2883:
2872:
2866:
2865:
2862:
2861:
2859:
2858:
2857:
2856:
2846:
2845:
2844:
2839:
2829:
2828:
2827:
2817:
2816:
2815:
2804:
2802:
2789:
2788:
2786:
2785:
2784:
2783:
2773:
2772:
2771:
2761:
2760:
2759:
2749:
2748:
2747:
2742:
2737:
2726:
2724:
2711:
2704:
2695:
2689:
2688:
2674:
2672:
2671:
2664:
2657:
2649:
2643:
2642:
2637:
2628:
2623:
2618:
2613:
2608:
2603:
2598:
2593:
2586:
2585:External links
2583:
2580:
2579:
2528:
2474:
2445:(6): 598–602.
2425:
2371:
2328:
2313:
2272:
2231:
2188:
2139:
2108:(24): 3892–8.
2088:
2062:
2037:
1981:
1974:
1956:
1925:(6): 380–381.
1905:
1870:
1843:
1800:
1773:(2): 138–140.
1757:
1726:
1673:
1630:
1609:(4): 1109–13.
1589:
1538:
1493:
1443:
1410:
1391:(4): 782–838.
1375:
1368:
1350:
1343:
1325:
1294:(2): a011684.
1274:
1233:
1207:
1200:
1182:
1169:(5): 251–256.
1149:
1098:
1071:(4): 498–503.
1050:
1032:
981:
975:978-0781773119
974:
954:
925:(12): 939–55.
902:
859:
852:
827:
809:
758:
751:
727:
726:
724:
721:
706:
703:
699:erythropoietin
651:Main article:
636:
633:
631:
628:
622:
619:
610:Main article:
607:
604:
594:
591:
589:
586:
584:values (MCH).
561:
558:
554:Haldane effect
534:
531:
518:
515:
503:
500:
489:
486:
476:
473:
435:
432:
307:
304:
239:) is the main
235:
231:
209:
208:
205:
204:
196:
191:
187:
186:
178:
173:
169:
168:
160:
155:
151:
150:
142:
137:
133:
132:
129:
126:
118:
117:
111:
107:
106:
100:
96:
95:
89:metalloprotein
86:
82:
81:
56:
48:
47:
43:
39:
38:(4 subunits, α
35:
34:
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
3395:
3384:
3381:
3379:
3376:
3374:
3371:
3369:
3366:
3365:
3363:
3350:
3349:
3342:
3336:
3335:Methemalbumin
3333:
3329:
3326:
3324:
3321:
3320:
3319:
3316:
3315:
3313:
3309:
3295:
3294:Leghemoglobin
3292:
3291:
3289:
3287:
3283:
3277:
3274:
3272:
3269:
3265:
3262:
3261:
3260:
3257:
3256:
3254:
3252:
3248:
3245:
3241:
3231:
3228:
3226:
3225:Chlorocruorin
3223:
3222:
3220:
3216:
3210:
3209:Methemoglobin
3207:
3205:
3202:
3201:
3199:
3195:
3189:
3186:
3184:
3180:
3179:Oxyhemoglobin
3177:
3175:
3172:
3170:
3167:
3166:
3164:
3160:
3141:
3138:
3127:
3124:
3113:
3110:
3099:
3096:
3085:
3082:
3075:
3072:
3065:
3062:
3061:
3059:
3057:
3053:
3034:
3031:
3020:
3014:
3003:
3000:
2999:
2997:
2993:
2978:
2975:
2964:
2961:
2960:
2958:
2954:
2939:
2936:
2925:
2922:
2911:
2908:
2897:
2894:
2893:
2891:
2887:
2884:
2882:
2876:
2873:
2871:
2867:
2855:
2852:
2851:
2850:
2847:
2843:
2840:
2838:
2835:
2834:
2833:
2830:
2826:
2823:
2822:
2821:
2818:
2814:
2811:
2810:
2809:
2806:
2805:
2803:
2801:
2799:
2795:
2790:
2782:
2779:
2778:
2777:
2774:
2770:
2767:
2766:
2765:
2762:
2758:
2755:
2754:
2753:
2750:
2746:
2743:
2741:
2738:
2736:
2733:
2732:
2731:
2728:
2727:
2725:
2723:
2721:
2715:
2712:
2708:
2705:
2703:
2699:
2696:
2694:
2690:
2685:
2681:
2678:that contain
2677:
2670:
2665:
2663:
2658:
2656:
2651:
2650:
2647:
2641:
2638:
2635:
2632:
2629:
2627:
2624:
2622:
2619:
2617:
2614:
2612:
2609:
2607:
2604:
2602:
2599:
2597:
2594:
2592:
2589:
2588:
2584:
2575:
2571:
2566:
2561:
2556:
2551:
2547:
2543:
2539:
2532:
2529:
2524:
2520:
2515:
2510:
2505:
2500:
2496:
2492:
2488:
2481:
2479:
2475:
2470:
2466:
2461:
2456:
2452:
2448:
2444:
2440:
2436:
2429:
2426:
2421:
2417:
2412:
2407:
2402:
2397:
2394:(3): 477–81.
2393:
2389:
2385:
2378:
2376:
2372:
2367:
2363:
2359:
2355:
2351:
2347:
2343:
2339:
2332:
2329:
2324:
2317:
2314:
2309:
2305:
2300:
2295:
2291:
2287:
2283:
2276:
2273:
2268:
2264:
2259:
2254:
2250:
2246:
2242:
2235:
2232:
2227:
2223:
2219:
2215:
2211:
2207:
2204:(6): 386–94.
2203:
2199:
2192:
2189:
2184:
2180:
2175:
2170:
2166:
2162:
2158:
2154:
2150:
2143:
2140:
2135:
2131:
2126:
2121:
2116:
2111:
2107:
2103:
2099:
2092:
2089:
2076:
2072:
2066:
2063:
2051:
2047:
2041:
2038:
2033:
2029:
2024:
2019:
2014:
2009:
2005:
2001:
1997:
1990:
1988:
1986:
1982:
1977:
1971:
1967:
1960:
1957:
1952:
1948:
1943:
1938:
1933:
1928:
1924:
1920:
1916:
1909:
1906:
1901:
1897:
1893:
1889:
1885:
1881:
1874:
1871:
1858:
1854:
1847:
1844:
1839:
1835:
1831:
1827:
1823:
1819:
1815:
1811:
1804:
1801:
1796:
1792:
1788:
1784:
1780:
1776:
1772:
1768:
1761:
1758:
1753:
1749:
1746:(3): 105–15.
1745:
1741:
1733:
1731:
1727:
1722:
1718:
1714:
1710:
1705:
1700:
1696:
1692:
1688:
1684:
1677:
1674:
1669:
1665:
1661:
1657:
1653:
1649:
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351:chromosome 11
348:
347:chromosome 16
343:
341:
340:two γ (gamma)
338:subunits and
337:
336:two α (alpha)
333:
329:
328:oxyhemoglobin
325:
321:
317:
316:hemoglobin A2
313:
305:
303:
301:
297:
293:
287:
285:
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261:
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246:in the human
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83:
77:
73:
68:
64:
60:
54:
49:
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19:
3345:
3323:Cytochrome b
3285:
3264:Metmyoglobin
3250:
3055:
3032:
2962:
2881:development:
2878:
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2807:
2792:
2775:
2763:
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2684:hemoproteins
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2497:(3): 412–9.
2494:
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2428:
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2387:
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2337:
2331:
2322:
2316:
2292:(2): 73–80.
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2244:
2234:
2201:
2197:
2191:
2159:(2): 217–9.
2156:
2152:
2142:
2105:
2101:
2091:
2079:. Retrieved
2074:
2065:
2054:. Retrieved
2049:
2040:
2006:(1): 19–27.
2003:
1999:
1968:. Elsevier.
1965:
1959:
1922:
1918:
1908:
1883:
1879:
1873:
1861:. Retrieved
1856:
1846:
1816:(2): 125–9.
1813:
1809:
1803:
1770:
1766:
1760:
1743:
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1646:(6): 534–8.
1643:
1639:
1633:
1606:
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1541:
1514:
1510:
1496:
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1459:
1430:(2): 84–89.
1427:
1423:
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1378:
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1353:
1334:
1328:
1291:
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1224:. Retrieved
1220:
1210:
1191:
1185:
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1115:
1111:
1101:
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1035:
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984:
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918:
872:
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842:
821:
775:
771:
761:
741:
708:
693:
682:
667:hemoglobin S
660:
656:
624:
615:
600:
596:
567:
563:
548:
544:
536:
524:
520:
505:
491:
466:
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423:
419:
411:
407:
401:codes for a
398:
390:
387:protein unit
382:
378:
374:
370:
364:
358:
344:
339:
335:
318:), has four
312:hemoglobin A
309:
288:
250:. Hemoglobin
229:
225:
222:hemoglobin F
221:
217:
213:
212:
125:Subunit name
85:Protein type
62:
58:
3373:Hemoglobins
3271:Neuroglobin
3197:Other human
2910:HbE Gower 2
2896:HbE Gower 1
1253:(2): 83–8.
712:bone marrow
695:Hydroxyurea
260:bloodstream
110:Cofactor(s)
3362:Categories
3318:Cytochrome
3276:Cytoglobin
3056:pathology:
2879:stages of
2794:Beta locus
2702:Hemoglobin
2056:2020-03-15
1880:Hemoglobin
1767:Hemoglobin
1704:2115/53256
1640:Hemoglobin
1018:1887/79403
965:Physiology
723:References
449:, (1976).
434:Production
276:hemoglobin
105:-transport
3346:see also
3259:Myoglobin
3162:Compounds
3033:HbF/Fetal
2963:HbF/Fetal
2889:Embryonic
2870:Tetramers
1689:: 124–7.
1501:Wood WG,
1001:: 43–53.
447:Wood W.G.
3218:Nonhuman
2710:Subunits
2676:Proteins
2574:25134627
2523:17595660
2469:16469830
2420:22735903
2366:22096967
2226:33180368
2218:17299377
2183:22139998
2134:24052549
2081:16 April
2032:21490337
1951:30559951
1863:15 March
1830:21473677
1795:13661613
1787:29745271
1721:23746089
1713:23073220
1668:41124341
1660:19958203
1584:26389678
1488:46171087
1480:17988294
1320:23378597
1269:21381239
1226:11 March
1144:26377141
1085:29610478
1042:Archived
1027:29032940
949:18458272
897:10820279
889:27801605
804:18988877
689:priapism
320:subunits
280:placenta
99:Function
93:globulin
3378:Infancy
2693:Globins
2565:4439869
2514:2360326
2460:1860403
2411:3405209
2358:1696840
2308:7677965
2267:7715639
2174:3302931
2125:3854110
2023:3139383
1942:6292363
1900:9859924
1838:5500015
1625:2435342
1575:4607133
1533:1100141
1405:4964061
1311:3552344
1135:4805326
1093:4690503
940:3256736
795:2581994
560:F-cells
403:glycine
395:alanine
199:Chr. 11
181:Chr. 11
163:Chr. 16
145:Chr. 16
3286:plant:
3251:human:
2745:pseudo
2572:
2562:
2521:
2511:
2467:
2457:
2418:
2408:
2364:
2356:
2306:
2265:
2224:
2216:
2181:
2171:
2132:
2122:
2030:
2020:
1972:
1949:
1939:
1898:
1836:
1828:
1793:
1785:
1752:810611
1750:
1719:
1711:
1666:
1658:
1623:
1582:
1572:
1531:
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1478:
1403:
1366:
1341:
1318:
1308:
1267:
1198:
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1132:
1091:
1083:
1025:
972:
947:
937:
895:
887:
850:
802:
792:
749:
675:sickle
284:uterus
272:
268:
264:
252:
241:oxygen
220:(also
103:oxygen
3311:Other
3243:Other
3074:Barts
2995:Adult
2956:Fetal
2362:S2CID
2222:S2CID
2102:Blood
2000:Blood
1834:S2CID
1791:S2CID
1717:S2CID
1664:S2CID
1603:Blood
1511:Blood
1484:S2CID
1089:S2CID
893:S2CID
772:Blood
355:genes
248:fetus
228:, or
216:, or
202:p15.4
190:Hb-γ2
184:p15.4
172:Hb-γ1
166:p13.3
154:Hb-α2
148:p13.3
136:Hb-α1
2854:HBE1
2842:HBG2
2837:HBG1
2769:HBQ1
2740:HBA2
2735:HBA1
2680:heme
2570:PMID
2519:PMID
2465:PMID
2416:PMID
2354:PMID
2338:Blut
2304:PMID
2263:PMID
2214:PMID
2179:PMID
2130:PMID
2083:2020
2028:PMID
1970:ISBN
1947:PMID
1896:PMID
1865:2020
1857:OMIM
1826:PMID
1783:PMID
1748:PMID
1709:PMID
1656:PMID
1621:PMID
1580:PMID
1529:PMID
1476:PMID
1401:PMID
1364:ISBN
1339:ISBN
1316:PMID
1265:PMID
1228:2020
1196:ISBN
1140:PMID
1081:PMID
1023:PMID
970:ISBN
945:PMID
885:PMID
848:ISBN
800:PMID
747:ISBN
576:and
424:HBG2
422:and
420:HBG1
412:HBA2
410:and
408:HBA1
399:HBG2
391:HBG1
383:HBG2
381:and
379:HBG1
375:HBA1
371:HBA2
366:HBA2
363:and
360:HBA1
324:heme
314:and
194:HBG2
176:HBG1
158:HBA2
140:HBA1
128:Gene
114:heme
76:4MQJ
67:heme
61:and
3140:HbO
3126:HbE
3112:HbC
3098:HbS
3084:HbD
3064:HbH
3016:HbA
3002:HbA
2977:HbA
2825:HBD
2813:HBB
2796:on
2781:HBM
2757:HBZ
2560:PMC
2550:doi
2546:172
2509:PMC
2499:doi
2455:PMC
2447:doi
2406:PMC
2396:doi
2392:107
2346:doi
2294:doi
2290:328
2253:doi
2249:332
2206:doi
2169:PMC
2161:doi
2120:PMC
2110:doi
2106:122
2018:PMC
2008:doi
2004:118
1937:PMC
1927:doi
1888:doi
1818:doi
1775:doi
1744:137
1699:hdl
1691:doi
1687:415
1648:doi
1611:doi
1570:PMC
1560:doi
1556:125
1519:doi
1468:doi
1432:doi
1393:doi
1306:PMC
1296:doi
1255:doi
1171:doi
1130:PMC
1120:doi
1073:doi
1013:hdl
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935:PMC
927:doi
923:148
877:doi
790:PMC
780:doi
776:112
529:).
226:HbF
116:(4)
72:PDB
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