The Andean goose is a member of the duck, goose and swan family Anatidae. It is also known as the wallata. It is in the shelduck subfamily Tadorninae.
Thalassemias are inherited blood disorders characterized by abnormal hemoglobin production. Symptoms depend on the type and can vary from none to severe. Often there is mild to severe anemia. Anemia can result in feeling tired and pale skin. There may also be bone problems, an enlarged spleen, yellowish skin, and dark urine. Slow growth may occur in children.
Fetal hemoglobin, or foetal haemoglobin, is the main oxygen transport protein in the human fetus during the last seven months of development in the uterus and persists in the newborn until roughly 2-4 months old. Functionally, fetal hemoglobin differs most from adult hemoglobin in that it is able to bind oxygen with greater affinity than the adult form, giving the developing fetus better access to oxygen from the mother's bloodstream.
Hemoglobin A (HbA), also known as adult hemoglobin, hemoglobin A1 or α2β2, is the most common human hemoglobin tetramer, accounting for over 97% of the total red blood cell hemoglobin. Hemoglobin is an oxygen-binding protein, found in erythrocytes, which transports oxygen from the lungs to the tissues. Hemoglobin A is the most common adult form of hemoglobin and exists as a tetramer containing two alpha subunits and two beta subunits (α2β2). Hemaglobin A2 (HbA2) is a less common adult form of hemoglobin and is composed of two alpha and two delta-globin subunits. This hemoglobin makes up 1-3% of hemoglobin in adults.
Hemoglobin A2 (HbA2) is a normal variant of hemoglobin A that consists of two alpha and two delta chains (α2δ2) and is found at low levels in normal human blood. Hemoglobin A2 may be increased in beta thalassemia or in people who are heterozygous for the beta thalassemia gene.
Beta thalassemias are a group of inherited blood disorders. They are forms of thalassemia caused by reduced or absent synthesis of the beta chains of hemoglobin that result in variable outcomes ranging from severe anemia to clinically asymptomatic individuals. Global annual incidence is estimated at one in 100,000. Beta thalassemias are caused by mutations in the HBB gene on chromosome 11, inherited in an autosomal recessive fashion. The severity of the disease depends on the nature of the mutation.
Hemoglobin variants are 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.
Hemoglobin subunit gamma-2 is a protein that in humans is encoded by the HBG2 gene.
Hemoglobin subunit delta is a protein that in humans is encoded by the HBD gene.
Hemoglobin subunit gamma-1 is a protein that in humans is encoded by the HBG1 gene.
Hemoglobin, alpha pseudogene 1, also known as HBAP1, is a human gene.
The human embryonic haemoglobins were discovered in 1961. These include Hb-Gower 1, consisting of 2 zeta chains and 2 epsilon chains, and Hb-Gower 2, which consists of 2 αlpha-chains and 2 epsilon-chains, the zeta and epsilon chains being the embryonic haemoglobin chains.
Hereditary persistence of fetal hemoglobin (HPFH) is a benign condition in which increased fetal hemoglobin production continues well into adulthood, disregarding the normal shutoff point after which only adult-type hemoglobin should be produced.
Delta-beta thalassemia is a form of thalassemia, and is autosomal recessive in terms of heredity. It is associated with hemoglobin subunit delta.
Hemoglobin, alpha 2 also known as HBA2 is a gene that in humans codes for the alpha globin chain of hemoglobin.
Hemorphin-4 is an endogenous opioid peptide of the hemorphin family which possesses antinociceptive properties and is derived from the β-chain of hemoglobin in the bloodstream. It is a tetrapeptide with the amino acid sequence Tyr-Pro-Trp-Thr. Hemorphin-4 has affinities for the μ-, δ-, and κ-opioid receptors that are in the same range as the structurally related β-casomorphins, although affinity to the κ-opioid receptor is markedly higher in comparison. It acts as an agonist at these sites. Hemorphin-4 also has inhibitory effects on angiotensin-converting enzyme (ACE), and as a result, may play a role in the regulation of blood pressure. Notably, inhibition of ACE also reduces enkephalin catabolism.
Hemorphins are a class of naturally occurring, endogenous opioid peptides which are found in the bloodstream, and are derived from the β-chain of hemoglobin. They have antinociceptive effects via activation of the opioid receptors, and some may also play a role in blood pressure through inhibition of the angiotensin-converting enzyme (ACE), as well as cause an elevation of endogenous enkephalin levels. Some examples of hemorphins include hemorphin-4, spinorphin, and valorphin.
Eukaryotic translation elongation factor 1 beta 2 pseudogene 1 (eEF1B1) is a protein that in humans is encoded by the EEF1B2P1 gene.
Eukaryotic translation elongation factor 1 beta 2 pseudogene 2 (eEF1B3) is a protein that in humans is encoded by the EEF1B2P2 gene.
Eukaryotic translation elongation factor 1 beta 2 pseudogene 3 (eEF1B4) is a protein that in humans is encoded by the EEF1B2P3 gene.
