Blood Substitutes and Oxygen Biotherapeutics 2022
DOI: 10.1007/978-3-030-95975-3_4
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Hemoglobin: Physiology and Hemoglobinopathy

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Cited by 5 publications
(8 citation statements)
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“…This study has shown that most of the children with SCD were coming from a family with a history of SCD thus, indicating that inheritable Haemoglobin disorders are common among the community in the Buhigwe district, Kigoma. A report by Yu and Mandal et al shows that over 12% worldwide population is at risk for Haemoglobin disorders and thus at least every clan and family has one child affected by sickle cell disease (SCD), sickle cell traits (SCT) or another abnormal hemoglobin gene (hemoglobin C or β-thalassemia) [13,24]. Finally, the presence of SCD among children from a family with no history of having SCD has been reported in this study.…”
Section: Discussionsupporting
confidence: 65%
“…This study has shown that most of the children with SCD were coming from a family with a history of SCD thus, indicating that inheritable Haemoglobin disorders are common among the community in the Buhigwe district, Kigoma. A report by Yu and Mandal et al shows that over 12% worldwide population is at risk for Haemoglobin disorders and thus at least every clan and family has one child affected by sickle cell disease (SCD), sickle cell traits (SCT) or another abnormal hemoglobin gene (hemoglobin C or β-thalassemia) [13,24]. Finally, the presence of SCD among children from a family with no history of having SCD has been reported in this study.…”
Section: Discussionsupporting
confidence: 65%
“…Hemoglobin is a tetrameric protein with two α- and two β-polypeptide chains; each chain has an iron-containing heme group, which is capable of binding one oxygen molecule. The oxygen dissociation curve displays a sigmoidal shape of the oxygen-binding equilibrium [ 13 ]. The oxygen-carrying iron in the hemoglobin molecule is normally in the reduced “ferrous” (Fe 2+ ) state; it is unable to bind oxygen if the hemoglobin molecule is oxidized to the “ferric” state (Fe 3+ ) to form methemoglobin (MetHb) [ 1 , 13 ].…”
Section: Hemoglobin-based Oxygen Carriers (Hbocs)mentioning
confidence: 99%
“…The oxygen dissociation curve displays a sigmoidal shape of the oxygen-binding equilibrium [ 13 ]. The oxygen-carrying iron in the hemoglobin molecule is normally in the reduced “ferrous” (Fe 2+ ) state; it is unable to bind oxygen if the hemoglobin molecule is oxidized to the “ferric” state (Fe 3+ ) to form methemoglobin (MetHb) [ 1 , 13 ]. The unique ability of hemoglobin molecules to undergo conformational changes enables the hemoglobin molecules to bind/load more oxygen in the lungs (higher oxygen affinity) and release more oxygen in the tissue capillaries (lower oxygen affinity).…”
Section: Hemoglobin-based Oxygen Carriers (Hbocs)mentioning
confidence: 99%
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“…Hemoglobin (Hb), the main O 2 carrier in RBCs, facilitates O 2 delivery via its well-known oxygen-carrying function [ 21 ]. In adults, Hb consist of four subunits (α1, β1, α2, and β2) that form a tetrameric protein containing a central ferrous heme, enabling it to transport O 2 by binding reversibly to O 2 [ 22 , 23 ].…”
Section: Introductionmentioning
confidence: 99%