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2,3-Bisphosphoglycerate
2,3-Bisphosphoglyceric acid (conjugate base 2,3-bisphosphoglycerate) (2,3-BPG), also known as 2,3-diphosphoglyceric acid (conjugate base 2,3-diphosphoglycerate) (2,3-DPG), is a three-carbon isomer of the glycolytic intermediate 1,3-bisphosphoglyceric acid (1,3-BPG). -2,3-BPG is present in human red blood cells (RBC; erythrocyte) at approximately 5 mmol/L. It binds with greater affinity to deoxygenated hemoglobin (e.g., when the red blood cell is near respiring tissue) than it does to oxygenated hemoglobin (e.g., in the lungs) due to conformational differences: 2,3-BPG (with an estimated size of about 9 Å) fits in the deoxygenated hemoglobin conformation (with an 11-Angstrom pocket), but not as well in the oxygenated conformation (5 Angstroms). It interacts with deoxygenated hemoglobin beta subunits and decreases the affinity for oxygen and allosterically promotes the release of the remaining oxygen molecules bound to the hemoglobin. Therefore, it enhances the ability of RB ...
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Phosphoglycerate Mutase
:''This enzyme is not to be confused with Bisphosphoglycerate mutase which catalyzes the conversion of 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate.'' Phosphoglycerate mutase (PGM) is any enzyme that catalyzes step 8 of glycolysis - the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme () is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM () class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Mechanism PGM is an isomerase enzyme, effectively transferring a phos ...
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Hemoglobin
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. In mammals, hemoglobin makes up about 96% of a red blood cell's dry matter, 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 ...
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Reinhold Benesch
Reinhold Benesch (August 13, 1919 – December 30, 1986) and Ruth Erica Benesch (February 25, 1925–March 25, 2000) were American biochemists at Columbia University whose forty year scientific collaboration primarily investigated hemoglobin. Their most important discovery was the function of 2,3-bisphosphoglyceric acid. Reinhold Benesch was born in Poland but immigrated to England. He graduated from Leeds University in 1941. Ruth Benesch was born in Paris, France to Helene Leroi, a German economist who returned with her to Berlin six days later. She and her sister were evacuated to England via Kindertransport in 1939, where she graduated from Stroud High School and received a B.Sc. from Birkbeck College in 1946. To support herself in college she worked at a rubber factory where she met Reinhold, who was working there as a consultant. They married in 1946. Both Benesches earned their doctorates in biochemistry from Northwestern University, he in 1950, she in 1952. They began ...
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Glycolysis
Glycolysis is the metabolic pathway that converts glucose () into pyruvic acid, pyruvate and, in most organisms, occurs in the liquid part of cells (the cytosol). The Thermodynamic free energy, free energy released in this process is used to form the high-energy molecules adenosine triphosphate (ATP) and NADH, reduced nicotinamide adenine dinucleotide (NADH). Glycolysis is a sequence of ten reactions catalyzed by enzymes. The wide occurrence of glycolysis in other species indicates that it is an ancient metabolic pathway. Indeed, the reactions that make up glycolysis and its parallel pathway, the pentose phosphate pathway, can occur in the Great Oxygenation Event, oxygen-free conditions of the Archean oceans, also in the absence of enzymes, catalyzed by metal ions, meaning this is a plausible prebiotic pathway for abiogenesis. The most common type of glycolysis is the ''Embden–Meyerhof–Parnas (EMP) pathway'', which was discovered by Gustav Embden, Otto Meyerhof, and Jakub Kar ...
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Bisphosphoglycerate Mutase
Bisphosphoglycerate mutase (, BPGM) is an enzyme expressed in erythrocytes and placental cells. It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. BPGM has both a mutase and a phosphatase function, but these are much less active, in contrast to its glycolytic cousin, phosphoglycerate mutase (PGM), which favors these two functions, but can also catalyze the synthesis of 2,3-BPG to a lesser extent. Tissue distribution Because the main function of bisphosphoglycerate mutase is the synthesis of 2,3-BPG, this enzyme is found only in erythrocytes and placental cells. In glycolysis, converting 1,3-BPG to 2,3-BPG bypasses the ATP-generating phosphoglycerate kinase reaction, consequently, no net ATP is generated when glucose is metabolized through the Luebering–Rapoport pathway. Since the main role of 2,3-BPG is to shift the equilibrium of hemoglobin toward the deoxy-state, its production is really only useful in ...
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Conjugate Acid
A conjugate acid, within the Brønsted–Lowry acid–base theory, is a chemical compound formed when an acid gives a proton () to a base—in other words, it is a base with a hydrogen ion added to it, as it loses a hydrogen ion in the reverse reaction. On the other hand, a conjugate base is what remains after an acid has donated a proton during a chemical reaction. Hence, a conjugate base is a substance formed by the removal of a proton from an acid, as it can gain a hydrogen ion in the reverse reaction. Because some acids can give multiple protons, the conjugate base of an acid may itself be acidic. In summary, this can be represented as the following chemical reaction: \text + \text \; \ce \; \text + \text Johannes Nicolaus Brønsted and Martin Lowry introduced the Brønsted–Lowry theory, which said that any compound that can give a proton to another compound is an acid, and the compound that receives the proton is a base. A proton is a subatomic particle in the n ...
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Metabolic Alkalosis
Metabolic alkalosis is an acid-base disorder in which the pH of tissue is elevated beyond the normal range (7.35–7.45). This is the result of decreased hydrogen ion concentration, leading to increased bicarbonate (), or alternatively a direct result of increased bicarbonate concentrations. The condition typically cannot last long if the kidneys are functioning properly. Signs and symptoms Severe metabolic alkalosis impacts multiple body systems, including the brain, muscles, heart, and lungs, and can cause various metabolic imbalances. Causes The causes of metabolic alkalosis can be divided into two categories, depending upon urine chloride levels. Chloride-responsive (Urine chloride < 25 mEq/L)

* Loss of hydrogen ions – Most often occurs via two mechanisms, either vomiting or via the kidney. ** results in the loss of

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High Altitude
Altitude is a distance measurement, usually in the vertical or "up" direction, between a reference datum and a point or object. The exact definition and reference datum varies according to the context (e.g., aviation, geometry, geographical survey, sport, or atmospheric pressure). Although the term ''altitude'' is commonly used to mean the height above sea level of a location, in geography the term elevation is often preferred for this usage. In aviation, altitude is typically measured relative to mean sea level or above ground level to ensure safe navigation and flight operations. In geometry and geographical surveys, altitude helps create accurate topographic maps and understand the terrain's elevation. For high-altitude trekking and sports, knowing and adapting to altitude is vital for performance and safety. Higher altitudes mean reduced oxygen levels, which can lead to altitude sickness if proper acclimatization measures are not taken. Vertical distance measurements in ...
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Hyperventilation
Hyperventilation is irregular breathing that occurs when the rate or tidal volume of breathing eliminates more carbon dioxide than the body can produce. This leads to hypocapnia, a reduced concentration of carbon dioxide dissolved in the blood. The body normally attempts to compensate for this homeostatically, but if this fails or is overridden, the blood pH will rise, leading to respiratory alkalosis. This increases the affinity of oxygen to hemoglobin and makes it harder for oxygen to be released into body tissues from the blood. The symptoms of respiratory alkalosis include dizziness, tingling in the lips, hands, or feet, headache, weakness, fainting, and seizures. In extreme cases, it may cause carpopedal spasms, a flapping and contraction of the hands and feet. Factors that may induce or sustain hyperventilation include: physiological stress, anxiety or panic disorder, high altitude, head injury, stroke, respiratory disorders such as asthma, pneumonia, or hyper ...
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Fetal Hemoglobin
Fetal hemoglobin, or foetal haemoglobin (also hemoglobin F, HbF, or α2γ2) is the main oxygen carrier protein in the human fetus. HemoglobinF is found in fetal red blood cells, and is involved in transporting oxygen from the mother's bloodstream to organs and tissues in the fetus. It is produced at around 6weeks of pregnancy and the levels remain high after birth until the baby is roughly 2–4months old. HemoglobinF has a different composition than adult forms of hemoglobin, 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 placenta found in the mother's uterus. 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 beta thalassemias, which affect components of the adult hemoglobin, can delay this ...
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