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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 RBC ...
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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. Hemoglobin F 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 6 weeks of pregnancy and the levels remain high after birth until the baby is roughly 2–4 months old. Hemoglobin F has a different composition from the adult forms of hemoglobin, which allows it to bind (or attach to) oxygen more strongly. This way, the developing fetus is able 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 del ...
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Allosterically
In biochemistry, allosteric regulation (or allosteric control) is the regulation of an enzyme by binding an effector molecule at a site other than the enzyme's active site. The site to which the effector binds is termed the ''allosteric site'' or ''regulatory site''. Allosteric sites allow effectors to bind to the protein, often resulting in a conformational change and/or a change in protein dynamics. Effectors that enhance the protein's activity are referred to as ''allosteric activators'', whereas those that decrease the protein's activity are called ''allosteric inhibitors''. Allosteric regulations are a natural example of control loops, such as feedback from downstream products or feedforward from upstream substrates. Long-range allostery is especially important in cell signaling. Allosteric regulation is also particularly important in the cell's ability to adjust enzyme activity. The term ''allostery'' comes from the Ancient Greek ''allos'' (), "other", and ''stere ...
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Bisphosphoglycerate Mutase
Bisphosphoglycerate mutase (, BPGM) is an enzyme unique to erythrocytes and placental cells. It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. BPGM also has 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 would be very inefficient, as it just adds another unnecessary step. 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 the cells which contain hemoglobin- erythrocytes and placental cells. Function 1,3-BPG is formed as ...
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1,3-Bisphosphoglyceric Acid
1,3-Bisphosphoglyceric acid (1,3-Bisphosphoglycerate or 1,3BPG) is a 3-carbon organic molecule present in most, if not all, living organisms. It primarily exists as a metabolic intermediate in both glycolysis during respiration and the Calvin cycle during photosynthesis. 1,3BPG is a transitional stage between glycerate 3-phosphate and glyceraldehyde 3-phosphate during the fixation/reduction of CO2. 1,3BPG is also a precursor to 2,3-bisphosphoglycerate which in turn is a reaction intermediate in the glycolytic pathway. Biological structure and role 1,3-Bisphosphoglycerate is the conjugate base of 1,3-bisphosphoglyceric acid. It is phosphorylated at the number 1 and 3 carbons. The result of this phosphorylation gives 1,3BPG important biological properties such as the ability to phosphorylate ADP to form the energy storage molecule ATP. In glycolysis As previously mentioned 1,3BPG is a metabolic intermediate in the glycolytic pathway. It is created by the exergonic oxidati ...
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Bisphosphoglycerate Phosphatase
In enzymology, a bisphosphoglycerate phosphatase () is an enzyme that catalyzes the chemical reaction :2,3-bisphospho-D-glycerate + H2O \rightleftharpoons 3-phospho-D-glycerate + phosphate Thus, the two substrates of this enzyme are 2,3-bisphospho-D-glycerate and H2O, whereas its two products are 3-phospho-D-glycerate and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 2,3-bisphospho-D-glycerate 2-phosphohydrolase. Other names in common use include 2,3-diphosphoglycerate phosphatase, diphosphoglycerate phosphatase, 2,3-diphosphoglyceric acid phosphatase, 2,3-bisphosphoglycerate phosphatase, and glycerate-2,3-diphosphate phosphatase. This enzyme participates in glycolysis/ gluconeogenesis. Structural studies As of late 2007, 7 structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or ...
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1,3-BPG
1,3-Bisphosphoglyceric acid (1,3-Bisphosphoglycerate or 1,3BPG) is a 3-carbon organic molecule present in most, if not all, living organisms. It primarily exists as a metabolic intermediate in both glycolysis during respiration and the Calvin cycle during photosynthesis. 1,3BPG is a transitional stage between glycerate 3-phosphate and glyceraldehyde 3-phosphate during the fixation/reduction of CO2. 1,3BPG is also a precursor to 2,3-bisphosphoglycerate which in turn is a reaction intermediate in the glycolytic pathway. Biological structure and role 1,3-Bisphosphoglycerate is the conjugate base of 1,3-bisphosphoglyceric acid. It is phosphorylated at the number 1 and 3 carbons. The result of this phosphorylation gives 1,3BPG important biological properties such as the ability to phosphorylate ADP to form the energy storage molecule ATP. In glycolysis As previously mentioned 1,3BPG is a metabolic intermediate in the glycolytic pathway. It is created by the exergonic oxida ...
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Bohr Effect
The Bohr effect is a phenomenon first described in 1904 by the Danish physiologist Christian Bohr. Hemoglobin's oxygen binding affinity (see oxygen–haemoglobin dissociation curve) is inversely related both to acidity and to the concentration of carbon dioxide. That is, the Bohr effect refers to the shift in the oxygen dissociation curve caused by changes in the concentration of carbon dioxide or the pH of the environment. Since carbon dioxide reacts with water to form carbonic acid, an increase in CO2 results in a decrease in blood pH, resulting in hemoglobin proteins releasing their load of oxygen. Conversely, a decrease in carbon dioxide provokes an increase in pH, which results in hemoglobin picking up more oxygen. Experimental discovery In the early 1900s, Christian Bohr was a professor at the University of Copenhagen in Denmark, already well known for his work in the field of respiratory physiology. He had spent the last two decades studying the solubility of oxygen, ...
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Congestive Heart Failure
Heart failure (HF), also known as congestive heart failure (CHF), is a syndrome, a group of signs and symptoms caused by an impairment of the heart's blood pumping function. Symptoms typically include shortness of breath, excessive fatigue, and leg swelling. The shortness of breath may occur with exertion or while lying down, and may wake people up during the night. Chest pain, including angina, is not usually caused by heart failure, but may occur if the heart failure was caused by a heart attack. The severity of the heart failure is measured by the severity of symptoms during exercise. Other conditions that may have symptoms similar to heart failure include obesity, kidney failure, liver disease, anemia, and thyroid disease. Common causes of heart failure include coronary artery disease, heart attack, high blood pressure, atrial fibrillation, valvular heart disease, excessive alcohol consumption, infection, and cardiomyopathy. These cause heart failure by altering ...
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Airway Obstruction
Airway obstruction is a blockage of respiration in the airway that hinders the free flow of air. It can be broadly classified into being either in the upper airway (UPA) or lower airway (LOA). Airway obstruction is a life-threatening condition and requires urgent attention, and assistance when it is needed. The assistance to clear an upper airway obstruction would begin employing first-aid anti-choking techniques. Upper airway obstruction Causes of upper airway obstruction include foreign body aspiration, blunt laryngotracheal trauma, penetrating laryngotracheal trauma, tonsillar hypertrophy, paralysis of the vocal cord or vocal fold, acute laryngotracheitis such as viral croup, bacterial tracheitis, epiglottitis, peritonsillar abscess, pertussis, retropharyngeal abscess, spasmodic croup. In basic and advanced life support airway obstructions are often referred to as ''A-problems''. Management of airways relies on both minimal-invasive and invasive techniques. Lower airw ...
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Molecular Symmetry
Molecular symmetry in chemistry describes the symmetry present in molecules and the classification of these molecules according to their symmetry. Molecular symmetry is a fundamental concept in chemistry, as it can be used to predict or explain many of a molecule's chemical properties, such as whether or not it has a dipole moment, as well as its allowed spectroscopic transitions. To do this it is necessary to use group theory. This involves classifying the states of the molecule using the irreducible representations from the character table of the symmetry group of the molecule. Symmetry is useful in the study of molecular orbitals, with applications to the Hückel method, to ligand field theory, and to the Woodward-Hoffmann rules. Many university level textbooks on physical chemistry, quantum chemistry, spectroscopy and inorganic chemistry discuss symmetry. Another framework on a larger scale is the use of crystal systems to describe crystallographic symmetry in bulk materia ...
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Carbon Dioxide
Carbon dioxide (chemical formula ) is a chemical compound made up of molecules that each have one carbon atom covalently double bonded to two oxygen atoms. It is found in the gas state at room temperature. In the air, carbon dioxide is transparent to visible light but absorbs infrared radiation, acting as a greenhouse gas. It is a trace gas in Earth's atmosphere at 421 parts per million (ppm), or about 0.04% by volume (as of May 2022), having risen from pre-industrial levels of 280 ppm. Burning fossil fuels is the primary cause of these increased CO2 concentrations and also the primary cause of climate change.IPCC (2022Summary for policy makersiClimate Change 2022: Mitigation of Climate Change. Contribution of Working Group III to the Sixth Assessment Report of the Intergovernmental Panel on Climate Change Cambridge University Press, Cambridge, United Kingdom and New York, NY, USA Carbon dioxide is soluble in water and is found in groundwater, lakes, ice caps, ...
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Myoglobin
Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. In humans, myoglobin is only found in the bloodstream after muscle injury. (Google books link is the 2008 edition) High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. Myoglobin is found in Type I muscle, Type II A, and Type II B; although many texts consider myoglobin not to be found in smooth muscle, this has proved erroneous: there is also myoglobin in smooth muscle cells. Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystal ...
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