GLP-1 receptor raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
This page was last updated on 2025-08-23 and is reviewed periodically as new material appears.
Three structural changes define the molecule. At position 8 an alpha-aminoisobutyric acid residue replaces alanine, which blocks dipeptidyl peptidase-4 cleavage. At position 34 arginine replaces lysine, and at position 26 a lysine carries a C18 fatty diacid attached through a short linker. The fatty chain binds serum albumin, and this albumin association reduces renal filtration and enzymatic attack. The unchanged backbone retains the receptor contacts that produce signalling. The free base has the formula C187H291N45O59 and a molecular weight near 4114 daltons.
Receptor activation follows the canonical Gs pathway: binding increases intracellular cyclic AMP, which promotes protein kinase A activity. In pancreatic beta cells this amplifies glucose-dependent insulin release, so secretion rises when blood glucose is high and changes little when it is low. The same signalling suppresses glucagon release from alpha cells and slows gastric emptying. Receptors in the hypothalamus and brainstem are thought to contribute to reduced appetite and lower energy intake. Which of these effects dominates clinical outcomes remains an area of active study.
Semaglutide is a synthetic peptide analogue of glucagon-like peptide-1, a gut hormone released by intestinal L cells after food intake. The natural hormone acts on pancreatic and central receptors but is degraded within minutes by dipeptidyl peptidase-4 and other peptidases. Semaglutide belongs to the class of long-acting GLP-1 receptor agonists, a group distinguished by structural changes that slow breakdown and extend circulation time. Its development followed earlier short-acting analogues and reflects a general strategy in peptide drug design: preserve receptor activity while blocking proteolytic clearance.
Semaglutide is a synthetic peptide that acts as an agonist at the glucagon-like peptide-1 receptor. It is a structural analogue of human GLP-1(7-37), modified to resist enzymatic degradation by dipeptidyl peptidase-4. The peptide backbone contains alpha-aminoisobutyric acid at position 8, a substitution that stabilises the helix and slows cleavage. A fatty diacid side chain attached through a linker at lysine 34 promotes binding to serum albumin, which extends the circulating half-life. These two modifications together allow less frequent administration than native GLP-1 requires.
Activation of the GLP-1 receptor couples to Gs signalling and raises intracellular cyclic AMP in pancreatic beta cells. The resulting insulin release depends on prevailing glucose concentrations, so the effect is greater when glucose is elevated. Receptor engagement also suppresses glucagon secretion and slows gastric emptying, which flattens post-meal glucose excursions. In the central nervous system, signalling in hypothalamic and brainstem regions is associated with reduced appetite and lower energy intake. Studies continue to examine effects on cardiac, renal and hepatic endpoints; whether those benefits are independent of weight change remains an open question.
Clinical development of this compound followed earlier short-acting GLP-1 analogues that required frequent injection. Once-weekly subcutaneous formulations entered use after 2017, and an oral formulation using a permeation enhancer later became available. The oral version pairs the peptide with sodium N-(8-[2-hydroxybenzoyl] amino) caprylate, a carrier that improves uptake across the gastric epithelium. Interest has expanded from glycaemic control into weight management and metabolic liver disease. Regulatory status and approved indications differ between countries, and the product remains subject to ongoing safety monitoring.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C187H291N45O59 | free base, without counter-ion |
| Molecular weight | About 4114 Da | peptide backbone plus attached lipid chain |
| Plasma half-life | About 165 hours | supports once-weekly dosing in humans |
| Plasma protein binding | Greater than 99 percent | attributed mainly to serum albumin |
| Receptor target | GLP-1 receptor | Gs-coupled, raises intracellular cyclic AMP |
Identity and purity are usually assessed by reverse-phase high-performance liquid chromatography coupled to mass spectrometry. Retention time and observed mass are compared against a reference standard run under identical conditions. Impurity profiles reveal deamidation products, oxidized methionine variants, and truncated fragments that arise during synthesis or storage. Peptide mapping through enzymatic digestion confirms the primary sequence, while amino acid analysis offers an independent check on overall composition.
Stability studies examine how temperature, pH, and moisture influence degradation rates over time. In aqueous solution, hydrolysis and deamidation accelerate as pH moves away from mildly acidic conditions. Light exposure and residual metal ions can also trigger oxidation of susceptible residues. Accelerated aging at elevated temperature is used to estimate shelf life, though extrapolation to room temperature carries uncertainty because individual degradation pathways do not always scale predictably.
Lyophilized semaglutide powder is typically held at minus twenty degrees Celsius for long-term storage. At that temperature, solid-state degradation reactions proceed slowly and the peptide remains intact for extended periods. Repeated freeze-thaw cycles are best avoided because they promote aggregation and can shift the proportion of monomeric peptide present. Working aliquots are often prepared so that each portion is thawed only once, and desiccant is placed inside the vial to limit moisture uptake.
Large randomised trials in adults with type 2 diabetes and in adults with obesity have reported reductions in body weight and improvements in several cardiovascular risk markers. One outcome trial found a lower incidence of major adverse cardiovascular events in participants with diabetes and established cardiovascular disease. Gastrointestinal effects such as nausea and vomiting are the most frequently reported adverse events and often diminish over time. Changes in lean body mass during weight loss are an area of ongoing investigation. Effects in adolescents and in pregnancy are less well characterised, and current labelling advises against use during pregnancy.
Semaglutide is a synthetic peptide analogue of glucagon-like peptide-1, a gut hormone released after nutrient intake. The molecule contains 31 amino acid residues and differs from the native sequence at several positions. A non-natural residue at position eight resists the enzyme that normally truncates the hormone, while a lysine-linked fatty diacid side chain promotes binding to serum albumin. These two modifications extend the circulating half-life from minutes to roughly one week. The peptide is produced by solid-phase synthesis followed by selective acylation, and its identity and purity are confirmed by spectrometric and chromatographic techniques.
The primary target is the GLP-1 receptor, a class B G protein-coupled receptor expressed on pancreatic beta cells, in the gut, and in several brain regions. Receptor activation raises intracellular cyclic AMP, which potentiates glucose-dependent insulin secretion and lowers glucagon release when blood glucose is elevated. Signalling in the hypothalamus and brainstem is associated with reduced appetite and slower gastric emptying. Because the insulinotropic effect depends on prevailing glucose levels, the hypoglycaemic risk of the peptide alone is described as low in most study settings. The relative contribution of peripheral and central actions remains an active research question.
Receptor binding triggers G protein signaling that raises intracellular cyclic AMP in pancreatic beta cells. Insulin release follows in a glucose-dependent manner, so secretion increases when blood glucose is elevated and diminishes when it is not. The same signaling suppresses glucagon release from alpha cells and slows gastric emptying, which blunts the post-meal glucose rise. In the brain, receptor activation in regions such as the arcuate nucleus is associated with reduced appetite and lower energy intake. How much each of these effects contributes to overall weight change is not fully settled.
Two structural features account for the prolonged half-life of semaglutide. A modified amino acid at position 8 resists cleavage by dipeptidyl peptidase-4, the enzyme that rapidly degrades native GLP-1. A fatty diacid side chain binds serum albumin, which limits renal clearance and protects the peptide from enzymatic breakdown. These modifications yield a plasma half-life of approximately one week in humans, allowing once-weekly administration. The relationship between plasma concentration and clinical effect varies between individuals, and sources of that variability are still being characterized.
Illinois Central Railroad number 51000 was built in the McComb, Mississippi shops with an aluminum superstructure to reduce weight with steel where required for strength and provided the standard dimensions, cushioned draft gear, easy-riding trucks, minimum 4 inches (10 cm) of insulation, adjustable ice bunker bulkheads and half-stage icing racks with forced air circulation through side wall flues and floor racks recommended by UFF&VA. Santa Fe Refrigerator Despatch number 13000 was built of stainless steel by the Consolidated Steel Corporation of Wilmington, California with convertible ice bunkers, side ventilation ducts, and axle-driven circulation fans. It was thought that stainless steel would better resist the corrosive deterioration resulting from salting the ice. The one-of-a-kind unit entered service as #13000, but was subsequently redesignated as #1300, and later given #4150 in 1955. The car spent most of its life in express service. Cost was cited as the reason no additional units were ordered. The car was dismantled at Clovis, New Mexico in February 1964. Pacific Fruit Express rebuilt two steel-sided ventilator refrigerator cars in their Los Angeles shops with aluminum car bodies to test the durability of lightweight alloys versus that of steel. It was hoped that weight savings (the units weighed almost 10,000 lb (4,536 kg) less than a like-sized all-steel car) and better corrosion resistance would offset the higher initial cost. Alcoa provided the body for number 44739, and Reynolds Aluminum Company provided number 45698.
Therefore, a large profit potential exists for the manufacturers and suppliers of processed food products. Individuals may see a benefit in convenience, but rarely see any direct financial cost benefit in using processed food as compared to home preparation. Processed food freed people from the large amount of time involved in preparing and cooking "natural" unprocessed foods. The increase in free time allows people much more choice in life style than previously allowed. In many families the adults are working away from home and therefore there is little time for the preparation of food based on fresh ingredients. The food industry offers products that fulfill many different needs: e.g. fully prepared ready meals that can be heated up in the microwave oven within a few minutes. Modern food processing also improves the quality of life for people with allergies, diabetics, and other people who cannot consume some common food elements. Food processing can also add extra nutrients such as vitamins.
=== EC 2.4.1: Hexosyltransferases === EC 2.4.1.1: Glycogen phosphorylase EC 2.4.1.2: dextrin dextranase EC 2.4.1.3: deleted, included in EC 2.4.1.25 EC 2.4.1.4: amylosucrase EC 2.4.1.5: dextransucrase EC 2.4.1.6: deleted EC 2.4.1.7: sucrose phosphorylase EC 2.4.1.8: maltose phosphorylase EC 2.4.1.9: inulosucrase EC 2.4.1.10: levansucrase EC 2.4.1.11: glycogen(starch) synthase EC 2.4.1.12: cellulose synthase (UDP-forming) EC 2.4.1.13: sucrose synthase EC 2.4.1.14: sucrose-phosphate synthase EC 2.4.1.15: α,α-trehalose-phosphate synthase (UDP-forming) EC 2.4.1.16: chitin synthase EC 2.4.1.17: glucuronosyltransferase EC 2.4.1.18: ,4-α-glucan branching enzyme EC 2.4.1.19: cyclomaltodextrin glucanotransferase EC 2.4.1.20: cellobiose phosphorylase EC 2.4.1.21: starch synthase EC 2.4.1.22: lactose synthase EC 2.4.1.23: sphingosine β-galactosyltransferase EC 2.4.1.24: 1,4-α-glucan 6-α-glucosyltransferase EC 2.4.1.25: 4-α-glucanotransferase EC 2.4.1.26: DNA α-glucosyltransferase EC 2.4.1.27: DNA β-glucosyltransferase EC 2.4.1.28: glucosyl-DNA β-glucosyltransferase EC 2.4.1.29: cellulose synthase (GDP-forming) EC 2.4.1.30: 1,3-β-oligoglucan phosphorylase EC 2.4.1.31: laminaribiose phosphorylase EC 2.4.1.32: glucomannan 4-β-mannosyltransferase EC 2.4.1.33: mannuronan synthase EC 2.4.1.34: 1,3-β-glucan synthase EC 2.4.1.35: phenol β-glucosyltransferase EC 2.4.1.36: α,α-trehalose-phosphate synthase (GDP-forming) EC 2.4.1.37: fucosylgalactoside 3-α-galactosyltransferase EC 2.4.1.38: β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase EC 2.4.1.39: steroid N-acetylglucosaminyltransferase EC 2.4.1.40: glycoprotein-fucosylgalactoside α-N-acetylgalactosaminyltransferase EC 2.4.1.41: polypeptide N-acetylgalactosaminyltransferase EC 2.4.1.42: deleted, included in EC 2.4.1.17 EC 2.4.1.43: polygalacturonate 4-α-galacturonosyltransferase EC 2.4.1.44: lipopolysaccharide 3-α-galactosyltransferase EC 2.4.1.45: now included with EC 2.4.1.47, N-acylsphingosine galactosyltransferase EC 2.4.1.46: monogalactosyldiacylglycerol synthase EC 2.4.1.47: N-acylsphingosine galactosyltransferase EC 2.4.1.48: heteroglycan α-mannosyltransferase EC 2.4.1.49: cellodextrin phosphorylase EC 2.4.1.50: procollagen galactosyltransferase EC 2.4.1.51: now covered by EC 2.4.1.101, EC 2.4.1.143, EC 2.4.1.144 and EC 2.4.1.145 EC 2.4.1.52: poly(glycerol-phosphate) α-glucosyltransferase EC 2.4.1.53: poly(ribitol-phosphate) β-glucosyltransferase EC 2.4.1.54: undecaprenyl-phosphate mannosyltransferase EC 2.4.1.55: Now EC 2.7.8.14, CDP-ribitol ribitolphosphotransferase EC 2.4.1.56: lipopolysaccharide N-acetylglucosaminyltransferase EC 2.4.1.57: Newer studies have shown that this is catalysed by two independent activities now covered by EC 2.4.1.345, phosphatidyl-myo-inositol α-mannosyl transferase and EC 2.4.1.346, phosphatidyl-myo-inositol dimannoside synthase EC 2.4.1.58: lipopolysaccharide glucosyltransferase I EC 2.4.1.59: deleted, included in EC 2.4.1.17 EC 2.4.1.60: CDP-abequose:α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase EC 2.4.1.61: deleted, included in EC 2.4.1.17 EC 2.4.1.62: ganglioside galactosyltransferase EC 2.4.1.63: linamarin synthase EC 2.4.1.64: α,α-trehalose phosphorylase EC 2.4.1.65: 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase EC 2.4.1.66: procollagen glucosyltransferase EC 2.4.1.67: galactinol—raffinose galactosyltransferase EC 2.4.1.68: glycoprotein 6-α-L-fucosyltransferase EC 2.4.1.69: type 1 galactoside α-(1,2)-fucosyltransferase EC 2.4.1.70: poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase EC 2.4.1.71: arylamine glucosyltransferase EC 2.4.1.72: now EC 2.4.2.24, 1,4-β-D-xylan synthase EC 2.4.1.73: lipopolysaccharide glucosyltransferase II EC 2.4.1.74: glycosaminoglycan galactosyltransferase EC 2.4.1.75: deleted entry, insufficient evidence to conclude that this is a different enzyme from EC 2.4.1.43 EC 2.4.1.76: deleted, included in EC 2.4.1.17 EC 2.4.1.77: deleted, included in EC 2.4.1.17 EC 2.4.1.78: phosphopolyprenol glucosyltransferase EC 2.4.1.79: globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase EC 2.4.1.80: ceramide glucosyltransferase EC 2.4.1.81: flavone 7-O-β-glucosyltransferase EC 2.4.1.82: galactinol—sucrose galactosyltransferase EC 2.4.1.83: dolichyl-phosphate β-D -mannosyltransferase EC 2.4.1.84: deleted, included in EC 2.4.1.17 EC 2.4.1.85: cyanohydrin β-glucosyltransferase EC 2.4.1.86: N-acetyl-β-D-glucosaminide β-(1,3)-galactosyltransferase EC 2.4.1.87: N-acetyllactosaminide 3-α-galactosyltransferase EC 2.4.1.88: globoside α-N-acetylgalactosaminyltransferase EC 2.4.1.89: deleted, included in EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase EC 2.4.1.90: N-acetyllactosamine synthase EC 2.4.1.91: flavonol 3-O-glucosyltransferase EC 2.4.1.92: (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase EC 2.4.1.93: Now EC 4.2.2.18, inulin fructotransferase (DFA-III-forming) EC 2.4.1.94: protein N-acetylglucosaminyltransferase EC 2.4.1.95: deleted EC 2.4.1.96: sn-glycerol-3-phosphate 1-galactosyltransferase EC 2.4.1.97: 1,3-β-D-glucan phosphorylase EC 2.4.1.98: deleted, Now included with EC 2.4.1.90, N-acetyllactosamine synthase EC 2.4.1.99: sucrose:sucrose fructosyltransferase EC 2.4.1.100: 2,1-fructan:2,1-fructan 1-fructosyltransferase EC 2.4.1.101: α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase EC 2.4.1.102: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase EC 2.4.1.103: alizarin 2-β-glucosyltransferase EC 2.4.1.104: o-dihydroxycoumarin 7-O-glucosyltransferase EC 2.4.1.105: vitexin β-glucosyltransferase EC 2.4.1.106: isovitexin β-glucosyltransferase EC 2.4.1.107: deleted, now included with EC 2.4.1.17, glucuronosyltransferase EC 2.4.1.108: deleted, now included with EC 2.4.1.17, glucuronosyltransferase EC 2.4.1.109: dolichyl-phosphate-mannose—protein mannosyltransferase EC 2.4.1.110: tRNA-queuosine β-mannosyltransferase EC 2.4.1.111: coniferyl-alcohol glucosyltransferase EC 2.4.1.112: The protein referred to in this entry is now known to be glycogenin so the entry has been incorporated into EC 2.4.1.186, glycogenin glucosyltransferase EC 2.4.1.113: α-1,4-glucan-protein synthase (ADP-forming) EC 2.4.1.114: 2-coumarate O-β-glucosyltransferase EC 2.4.1.115: anthocyanidin 3-O-glucosyltransferase EC 2.4.1.116: cyanidin 3-O-rutinoside 5-O-glucosyltransferase EC 2.4.1.117: dolichyl-phosphate β-glucosyltransferase EC 2.4.1.118: cytokinin 7-β-glucosyltransferase EC 2.4.1.119: transferred to EC 2.4.99.18, dolichyl-diphosphooligosaccharideprotein glycotransferase EC 2.4.1.120: sinapate 1-glucosyltransferase EC 2.4.1.121: indole-3-acetate β-glucosyltransferase EC 2.4.1.122: N-acetylgalactosaminide β-1,3-galactosyltransferase EC 2.4.1.123: inositol 3-α-galactosyltransferase EC 2.4.1.124: Now EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase EC 2.4.1.125: sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase EC 2.4.1.126: hydroxycinnamate 4-β-glucosyltransferase EC 2.4.1.127: monoterpenol β-glucosyltransferase EC 2.4.1.128: scopoletin glucosyltransferase EC 2.4.1.129: peptidoglycan glycosyltransferase EC 2.4.1.130: Now covered by EC 2.4.1.258, EC 2.4.1.259, EC 2.4.1.260 and EC 2.4.1.261 EC 2.4.1.131: GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase EC 2.4.1.132: GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase EC 2.4.1.133: xylosylprotein 4-β-galactosyltransferase EC 2.4.1.134: galactosylxylosylprotein 3-β-galactosyltransferase EC 2.4.1.135: galactosylgalactosylxylosylprotein 3-β-glucuronosyltransferase EC 2.4.1.136: gallate 1-β-glucosyltransferase EC 2.4.1.137: sn-glycerol-3-phosphate 2-α-galactosyltransferase EC 2.4.1.138: mannotetraose 2-α-N-acetylglucosaminyltransferase EC 2.4.1.139: maltose synthase EC 2.4.1.140: alternansucrase EC 2.4.1.141: N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase EC 2.4.1.142: chitobiosyldiphosphodolichol β-mannosyltransferase EC 2.4.1.143: α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase EC 2.4.1.144: β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase EC 2.4.1.145: α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase EC 2.4.1.146: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase EC 2.4.1.147: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase EC 2.4.1.148: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase EC 2.4.1.149: N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase EC 2.4.1.150: N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase EC 2.4.1.151: now included with EC 2.4.1.87 N-acetyllactosaminide 3-α-galactosyltransferase EC 2.4.1.152: 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase EC 2.4.1.153: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminyltransferase EC 2.4.1.154: identical to EC 2.4.1.79, globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase EC 2.4.1.155: α-1,6-mannosyl-glycoprotein 6-β-N-acetylglucosaminyltransferase EC 2.4.1.156: indolylacetyl-myo-inositol galactosyltransferase EC 2.4.1.157: 1,2-diacylglycerol 3-glucosyltransferase, now classified as EC 2.4.1.336, monoglucosyldiacylglycerol synthase, and EC 2.4.1.337, 1,2-diacylglycerol 3-α-glucosyltransferase EC 2.4.1.158: 13-hydroxydocosanoate 13-β-glucosyltransferase EC 2.4.1.159: flavonol-3-O-glucoside L-rhamnosyltransferase EC 2.4.1.160: pyridoxine 5′-O-β-D-glucosyltransferase EC 2.4.1.161: oligosaccharide 4-α-D-glucosyltransferase EC 2.4.1.162: aldose β-D-fructosyltransferase EC 2.4.1.163: now included in EC 2.4.1.149, N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase EC 2.4.1.164: now included with EC 2.4.1.150, N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase EC 2.4.1.165: N-acetylneuraminylgalactosylglucosylceramide β-1,4-N-acetylgalactosaminyltransferase EC 2.4.1.166: raffinose—raffinose α-galactosyltransferase EC 2.4.1.167: sucrose 6F-α-galactosyltransferase EC 2.4.1.168: xyloglucan 4-glucosyltransferase EC 2.4.1.169: now EC 2.4.2.39, xyloglucan 6-xylosyltransferase EC 2.4.1.170: isoflavone 7-O-glucosyltransferase EC 2.4.1.171: methyl-ONN-azoxymethanol β-D-glucosyltransferase EC 2.4.1.172: salicyl-alcohol β-D-glucosyltransferase EC 2.4.1.173: sterol 3β-glucosyltransferase EC 2.4.1.174: glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase EC 2.4.1.175: glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase EC 2.4.1.176: gibberellin β-D-glucosyltransferase EC 2.4.1.177: cinnamate β-D-glucosyltransferase EC 2.4.1.178: hydroxymandelonitrile glucosyltransferase EC 2.4.1.179: lactosylceramide β-1,3-galactosyltransferase EC 2.4.1.180: lipopolysaccharide N-acetylmannosaminouronosyltransferase EC 2.4.1.181: hydroxyanthraquinone glucosyltransferase EC 2.4.1.182: lipid-A-disaccharide synthase EC 2.4.1.183: α-1,3-glucan synthase EC 2.4.1.184: galactolipid galactosyltransferase EC 2.4.1.185: flavanone 7-O-β-glucosyltransferase EC 2.4.1.186: glycogenin glucosyltransferase EC 2.4.1.187: N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-β-D-mannosaminyltransferase EC 2.4.1.188: N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase EC 2.4.1.189: uteolin 7-O-glucuronosyltransferase EC 2.4.1.190: luteolin-7-O-glucuronide 2′′-O-glucuronosyltransferase EC 2.4.1.191: luteolin-7-O-diglucuronide 4′-O-glucuronosyltransferase EC 2.4.1.192: nuatigenin 3β-glucosyltransferase EC 2.4.1.193: sarsapogenin 3β-glucosyltransferase EC 2.4.1.194: 4-hydroxybenzoate 4-O-β-D-glucosyltransferase EC 2.4.1.195: N-hydroxythioamide S-β-glucosyltransferase EC 2.4.1.196: nicotinate glucosyltransferase EC 2.4.1.197: high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase EC 2.4.1.198: phosphatidylinositol N-acetylglucosaminyltransferase EC 2.4.1.199: β-mannosylphosphodecaprenol—mannooligosaccharide 6-mannosyltransferase EC 2.4.1.200: now EC 4.2.2.17, inulin fructotransferase (DFA-I-forming) EC 2.4.1.201: α-1,6-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase EC 2.4.1.202: 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase EC 2.4.1.203: trans-zeatin O-β-D-glucosyltransferase EC 2.4.1.204: now EC 2.4.2.40, zeatin O-β-D-xylosyltransferase EC 2.4.1.205: galactogen 6β-galactosyltransferase EC 2.4.1.206: lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase EC 2.4.1.207: xyloglucan:xyloglucosyl transferase EC 2.4.1.208: diglucosyl diacylglycerol synthase (1,2-linking) EC 2.4.1.209: cis-p-coumarate glucosyltransferase EC 2.4.1.210: limonoid glucosyltransferase EC 2.4.1.211: 1,3-β-galactosyl-N-acetylhexosamine phosphorylase EC 2.4.1.212: hyaluronan synthase EC 2.4.1.213: glucosylglycerol-phosphate synthase EC 2.4.1.214: glycoprotein 3-α-L-fucosyltransferase EC 2.4.1.215: cis-zeatin O-β-D-glucosyltransferase EC 2.4.1.216: trehalose 6-phosphate phosphorylase EC 2.4.1.217: mannosyl-3-phosphoglycerate synthase EC 2.4.1.218: hydroquinone glucosyltransferase EC 2.4.1.219: vomilenine glucosyltransferase EC 2.4.1.220: indoxyl-UDPG glucosyltransferase EC 2.4.1.221: peptide-O-fucosyltransferase EC 2.4.1.222: O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase EC 2.4.1.223: glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase EC 2.4.1.224: glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase EC 2.4.1.225: N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase EC 2.4.1.226: N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase EC 2.4.1.227: undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase EC 2.4.1.228: lactosylceramide 4-α-galactosyltransferase EC 2.4.1.229: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase EC 2.4.1.230: kojibiose phosphorylase EC 2.4.1.231: α,α-trehalose phosphorylase (configuration-retaining) EC 2.4.1.232: initiation-specific α-1,6-mannosyltransferase EC 2.4.1.233: deleted: identical to EC 2.4.1.115, anthocyanidin 3-O-glucosyltransferase EC 2.4.1.234: kaempferol 3-O-galactosyltransferase EC 2.4.1.235: deleted: identical to EC 2.4.1.116, cyanidin 3-O-rutinoside 5-O-glucosyltransferase EC 2.4.1.236: flavanone 7-O-glucoside 2′′-O-β-L-rhamnosyltransferase EC 2.4.1.237: flavonol 7-O-β-glucosyltransferase EC 2.4.1.238: delphinidin 3,5-di-O-glucoside 3′-O-glucosyltransferase EC 2.4.1.239: flavonol-3-O-glucoside glucosyltransferase EC 2.4.1.240: flavonol-3-O-glycoside glucosyltransferase EC 2.4.1.241: flavonol-3-O-glycoside glucosyltransferase EC 2.4.1.242: NDP-glucose—starch glucosyltransferase EC 2.4.1.243: 6G-fructosyltransferase EC 2.4.1.244: N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase EC 2.4.1.245: α,α-trehalose synthase EC 2.4.1.246: mannosylfructose-phosphate synthase EC 2.4.1.247: β-D-galactosyl-(1→4)-L-rhamnose phosphorylase EC 2.4.1.248: cycloisomaltooligosaccharide glucanotransferase EC 2.4.1.249: delphinidin 3′,5′-O-glucosyltransferase EC 2.4.1.250: D-inositol-3-phosphate glycosyltransferase EC 2.4.1.251: GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol 4-β-mannosyltransferase EC 2.4.1.252: GDP-mannose:cellobiosyl-diphosphopolyprenol α-mannosyltransferase EC 2.4.1.253: baicalein 7-O-glucuronosyltransferase EC 2.4.1.254: cyanidin-3-O-glucoside 2′′-O-glucuronosyltransferase EC 2.4.1.255: protein O-GlcNAc transferase EC 2.4.1.256: dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase EC 2.4.1.257: GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase EC 2.4.1.258: dolichyl-P-Man:Man5GlcNAc2-PP-dolichol α-1,3-mannosyltransferase EC 2.4.1.259: dolichyl-P-Man:Man6GlcNAc2-PP-dolichol α-1,2-mannosyltransferase EC 2.4.1.260: dolichyl-P-Man:Man7GlcNAc2-PP-dolichol α-1,6-mannosyltransferase EC 2.4.1.261: dolichyl-P-Man:Man8GlcNAc2-PP-dolichol α-1,2-mannosyltransferase EC 2.4.1.262: soyasapogenol glucuronosyltransferase EC 2.4.1.263: abscisate β-glucosyltransferase EC 2.4.1.264: D-Man-α-(1→3)-D-Glc-β-(1→4)-DD-Glc-α-1-diphosphoundecaprenol 2-β-glucuronosyltransferase EC 2.4.1.265: olichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase EC 2.4.1.266: glucosyl-3-phosphoglycerate synthase EC 2.4.1.267: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase EC 2.4.1.268: glucosylglycerate synthase EC 2.4.1.269: mannosylglycerate synthase EC 2.4.1.270: mannosylglucosyl-3-phosphoglycerate synthase EC 2.4.1.271: crocetin glucosyltransferase EC 2.4.1.272: soyasapogenol B glucuronide galactosyltransferase EC 2.4.1.273: soyasaponin III rhamnosyltransferase EC 2.4.1.274: glucosylceramide β-1,4-galactosyltransferase EC 2.4.1.275: neolactotriaosylceramide β-1,4-galactosyltransferase EC 2.4.1.276: zeaxanthin glucosyltransferase EC 2.4.1.277: glycosyltransferase DesVII EC 2.4.1.278: desosaminyl transferase EryCIII EC 2.4.1.279: nigerose phosphorylase EC 2.4.1.280: N,N′-diacetylchitobiose phosphorylase EC 2.4.1.281: 4-O-β-D-mannosyl-D-glucose phosphorylase EC 2.4.1.282: 3-O-α-D-glucosyl-L-rhamnose phosphorylase EC 2.4.1.283: 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase EC 2.4.1.284: 2-deoxystreptamine glucosyltransferase EC 2.4.1.285: UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase EC 2.4.1.286: chalcone 4′-O-glucosyltransferase EC 2.4.1.287: rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,4/1,5-galactofuranosyltransferase EC 2.4.1.288: galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,5/1,6-galactofuranosyltransferase EC 2.4.1.289: N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase EC 2.4.1.290: N,N′-diacetylbacillosaminyl-diphospho-undecaprenol α-1,3-N-acetylgalactosaminyltransferase EC 2.4.1.291: N-acetylgalactosamine-N,N′-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase EC 2.4.1.292: GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase EC 2.4.1.293: GalNAc5-diNAcBac-PP-undecaprenol β-1,3-glucosyltransferase EC 2.4.1.294: cyanidin 3-O-galactosyltransferase EC 2.4.1.295: anthocyanin 3-O-sambubioside 5-O-glucosyltransferase EC 2.4.1.296: anthocyanidin 3-O-coumaroylrutinoside 5-O-glucosyltransferase EC 2.4.1.297: anthocyanidin 3-O-glucoside 2′′-O-glucosyltransferase EC 2.4.1.298: anthocyanidin 3-O-glucoside 5-O-glucosyltransferase EC 2.4.1.299: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose) EC 2.4.1.300: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose) EC 2.4.1.301: 2′-deamino-2′-hydroxyneamine 1-α-D-kanosaminyltransferase EC 2.4.1.302: L-demethylnoviosyl transferase EC 2.4.1.303: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase EC 2.4.1.304: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase EC 2.4.1.305: UDP-Glc:α-D-GlcNAc-glucosaminyl-diphosphoundecaprenol β-1,3-glucosyltransferase EC 2.4.1.306: UDP-GalNAc:α-D-GalNAc-diphosphoundecaprenol α-1,3-N-acetylgalactosaminyltransferase EC 2.4.1.307: UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase. Now included in EC 2.4.1.122, N-acetylgalactosaminide β-1,3-galactosyltransferase EC 2.4.1.308: GDP-Fuc:β-D-Gal-1,3-α-D-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,2-fucosyltransferase EC 2.4.1.309: UDP-Gal:α-L-Fuc-1,2-β-Gal-1,3-α-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,3-galactosyltransferase EC 2.4.1.310: vancomycin aglycone glucosyltransferase EC 2.4.1.311: chloroorienticin B synthase EC 2.4.1.312: protein O-mannose β-1,4-N-acetylglucosaminyltransferase EC 2.4.1.313: protein O-mannose β-1,3-N-acetylgalactosaminyltransferase EC 2.4.1.314: ginsenoside Rd glucosyltransferase EC 2.4.1.315: diglucosyl diacylglycerol synthase (1,6-linking) EC 2.4.1.316: tylactone mycaminosyltransferase EC 2.4.1.317: O-mycaminosyltylonolide 6-deoxyallosyltransferase EC 2.4.1.318: demethyllactenocin mycarosyltransferase EC 2.4.1.319: β-1,4-mannooligosaccharide phosphorylase EC 2.4.1.320: 1,4-β-mannosyl-N-acetylglucosamine phosphorylase EC 2.4.1.321: cellobionic acid phosphorylase EC 2.4.1.322: devancosaminyl-vancomycin vancosaminetransferase EC 2.4.1.323: 7-deoxyloganetic acid glucosyltransferase EC 2.4.1.324: 7-deoxyloganetin glucosyltransferase EC 2.4.1.325: TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase EC 2.4.1.326: aklavinone 7-L-rhodosaminyltransferase EC 2.4.1.327: aclacinomycin-T 2-deoxy-L-fucose transferase EC 2.4.1.328: erythronolide mycarosyltransferase EC 2.4.1.329: sucrose 6F-phosphate phosphorylase EC 2.4.1.330: β-D-glucosyl crocetin β-1,6-glucosyltransferase EC 2.4.1.331: 8-demethyltetracenomycin C L-rhamnosyltransferase EC 2.4.1.332: 1,2-α-glucosylglycerol phosphorylase EC 2.4.1.333: 1,2-β-oligoglucan phosphorylase EC 2.4.1.334: 1,3-α-oligoglucan phosphorylase EC 2.4.1.335: dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase EC 2.4.1.336: monoglucosyldiacylglycerol synthase EC 2.4.1.337: 1,2-diacylglycerol 3-α-glucosyltransferase EC 2.4.1.338: validoxylamine A glucosyltransferase EC 2.4.1.339: β-1,2-mannobiose phosphorylase EC 2.4.1.340: 1,2-β-oligomannan phosphorylase EC 2.4.1.341: α-1,2-colitosyltransferase EC 2.4.1.342: α-maltose-1-phosphate synthase EC 2.4.1.343: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase EC 2.4.1.344: type 2 galactoside α-(1,2)-fucosyltransferase EC 2.4.1.345: phosphatidyl-myo-inositol α-mannosyltransferase EC 2.4.1.346: phosphatidyl-myo-inositol dimannoside synthase EC 2.4.1.347: α,α-trehalose-phosphate synthase (ADP-forming) EC 2.4.1.348: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase EC 2.4.1.349: mannosyl-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase EC 2.4.1.350: mogroside IE synthase EC 2.4.1.351: rhamnogalacturonan I rhamnosyltransferase EC 2.4.1.352: glucosylglycerate phosphorylase EC 2.4.1.353: sordaricin 6-deoxyaltrosyltransferase EC 2.4.1.354: (R)-mandelonitrile β-glucosyltransferase EC 2.4.1.355: poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase EC 2.4.1.356: glucosyl-dolichyl phosphate glucuronosyltransferase EC 2.4.1.357: phlorizin synthase EC 2.4.1.358: acylphloroglucinol glucosyltransferase EC 2.4.1.359: glucosylglycerol phosphorylase (configuration-retaining) EC 2.4.1.360: 2-hydroxyflavanone C-glucosyltransferase EC 2.4.1.361: GDP-mannose:di-myo-inositol-1,3′-phosphate β-1,2-mannosyltransferase EC 2.4.1.362: α-(1→3) branching sucrase EC 2.4.1.363: ginsenoside 20-O-glucosyltransferase EC 2.4.1.364: protopanaxadiol-type ginsenoside 3-O-glucosyltransferase EC 2.4.1.365: protopanaxadiol-type ginsenoside-3-O-glucoside 2′′-O-glucosyltransferase EC 2.4.1.366: ginsenoside F1 6-O-glucosyltransferase EC 2.4.1.367: ginsenoside 6-O-glucosyltransferase EC 2.4.1.368: oleanolate 3-O-glucosyltransferase EC 2.4.1.369: enterobactin C-glucosyltransferase EC 2.4.1.370: inositol phosphorylceramide mannosyltransferase EC 2.4.1.371: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-α-mannosylpolymerase EC 2.4.1.372: mutansucrase EC 2.4.1.373: α-(1→2) branching sucrase EC 2.4.1.374: β-1,2-mannooligosaccharide synthase EC 2.4.1.375: rhamnogalacturonan I galactosyltransferase EC 2.4.1.376: EGF-domain serine glucosyltransferase EC 2.4.1.377: dTDP-Rha:α-D-Gal-diphosphoundecaprenol α-1,3-rhamnosyltransferase EC 2.4.1.378: GDP-mannose:α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,4-mannosyltransferase EC 2.4.1.379: GDP-Man:α-D-Gal-diphosphoundecaprenol α-1,3-mannosyltransferase EC 2.4.1.380: GDP-Man:α-D-Man-(1→3)-α-D-Gal diphosphoundecaprenol α-1,2-mannosyltransferase EC 2.4.1.381: dTDP-Rha:α-D-Man-(1→3)-α-D-Gal diphosphoundecaprenol α-1,2-rhamnosyltransferase EC 2.4.1.382: CDP-abequose:α-L-Rha2OAc-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase EC 2.4.1.383: GDP-Man:α-L-Rha-(1→3)-α-D-Gal-PP-Und β-1,4-mannosyltransferase EC 2.4.1.384: NDP-glycosyltransferase
Sources: en.wikipedia.org
Cardiovascular Bradycardia Bundle branch blocks Complete heart block and arrhythmias Cardiomegaly Elevated diastolic blood pressure—early Hypotension—late Low cardiac output Non-specific ECG findings Pericardial effusion Polymorphic ventricular tachycardia (torsades de pointes) Prolonged QT interval Respiratory Hypoxia Hypercapnia Hyperventilation Myxedema of the larynx Pleural effusion Gastrointestinal Abdominal distention Abdominal pain Anasarca Anorexia and nausea Decreased motility Fecal impaction and constipation Gastrointestinal atony or ileus Myxedema or toxic megacolon—late Neurogenic oropharyngeal dysphagia ileus Neurological Altered mentation Coma Confusion and obtundation Delayed tendon reflexes Depression Poor cognitive function Psychosis Seizures Renal and urinary function Bladder dystonia and distension Fluid retention Appearance and dermatological Alopecia Coarse, sparse hair Dry, cool, doughy skin Myxedematous face Generalized swelling Goiter Macroglossia Non-pitting edema Ptosis Periorbital edema Surgical scar from prior thyroidectomy Hypothermia (often marked: usually < 35 °C/ 95 °F) Laboratory features in myxedema coma:
=== Fourth week (14–18 March) === On 14 March, the Taliban-run Afghan Ministry of Defense said that Taliban forces had captured a Pakistani border outpost, killing 14 soldiers and injuring 11 others. The ministry also added that they destroyed an armored tank and a military vehicle of Pakistani forces. However, Pakistani officials denied allegations made by Afghan Ministry of Defense, terming them false, fabricated and aimed at misleading the Afghan public. According to Pakistani officials, the damages and losses suffered by the Afghan Taliban and the Pakistani Taliban were being regularly documented, with related video and photographic evidence shared with the media. Elsewhere, Pakistani security forces killed six Pakistani Taliban militants in Lakki Marwat. Later that day, Pakistani officials stated that the Pakistan Air Force had carried out airstrikes on five military bases in Kandahar, including the General Directorate of Intelligence (GDI), Haibatullah Akhundzada's special forces unit, the border command, a tunnel, and a Taliban technical equipment warehouse. Pakistani officials added that the targeted military sites had been destroyed and released videos and images of the strikes in Kandahar. Locals in Kandahar told an Agence France-Presse journalist that military aircraft had flown over a mountain housing a military facility before an explosion was heard. Afghan locals sources state that Pakistani airstrikes struck a Taliban special forces facility linked to Hibatullah Akhundzada, as well as an ammunition depot and a border command center in Kandahar Province.
Lying in the perineum (space between the vulva and anus) and within the superficial perineal pouch is the root of the clitoris, which consists of the posterior ends of the clitoris, the crura and the bulbs of vestibule. The crura ("legs") are the parts of the corpora cavernosa extending from the clitoral body and form an upside-down "V" shape. Each crus (singular form of crura) is attached to the corresponding ischial ramus – extensions of the corpora beneath the descending pubic rami. Concealed behind the labia minora, the crura end with attachment at or just below the middle of the pubic arch. Associated are the urethral sponge, perineal sponge, a network of nerves and blood vessels, the suspensory ligament of the clitoris, muscles and the pelvic floor. The vestibular bulbs are more closely related to the clitoris than the vestibule because of the similarity of the trabecular and erectile tissue within the clitoris and its bulbs, and the absence of trabecular tissue in other parts of the vulva, with the erectile tissue's trabecular nature allowing engorgement and expansion during sexual arousal. The vestibular bulbs are typically described as lying close to the crura on either side of the vaginal opening; internally, they are beneath the labia majora. The anterior sections of the bulbs unite to create the bulbar commissure, which forms a long strip of erectile tissue dubbed the infra-corporeal residual spongy part (RSP) that expands from the ventral shaft and terminates as the glans.
== Prevention == Military data suggest that the risk of exertional rhabdomyolysis can be lowered by engaging in prolonged lower-intensity exercise, as opposed to high-intensity exercise over a shorter time period. In all athletic programs, three features should be present: (1) emphasizing prolonged lower-intensity exercise, as opposed to repetitive max intensity exercises; (2) adequate rest periods and a high-carbohydrate diet, to replenish glycogen stores; and (3) proper hydration, to enhance renal clearance of myoglobin. Also, exercise in above-average temperature and humidity can increase risk for ER. ER can be avoided by gradually increasing intensity during new exercise regimens, properly hydrating, acclimatization, and avoidance of diuretics during times of strenuous activity.
Sources: en.wikipedia.org
(2) The study of Raymond Damadian (New York Downstate Medical Center, 1971-1972): Inspired by Hazlewood and Chang's findings about cellular water relaxation time changes during muscle development, Damadian proposed that T1 is generally longer in tumors compared to normal tissues. He demonstrated this idea with a quick NMR measurement on rat tissues. Damadian also filed a patent in late 1972 for a full-body machine of using NMR to detect cancer. (3) The study of Paul Lauterbur (The State University of New York at Stony Brook, 1973): Lauterbur proposed to use a magnetic field gradient to conduct a 2-dimensional NMR scan. He called his method zeugmatography. For demonstration, he used CW NMR (not spin-echo) to image the proton spin density in an artificial sample consisting of two tubes of water. In the late 1970s, physicists Peter Mansfield at the University of Nottingham and Lauterbur developed MRI-related techniques, like the echo-planar imaging (EPI) technique. Raymond Damadian's work into nuclear magnetic resonance (NMR) has been incorporated into MRI, having built one of the first scanners. Advances in semiconductor technology were crucial to the development of practical MRI, which requires a large amount of computational power. This was made possible by the rapidly increasing number of transistors on a single integrated circuit chip. Mansfield and Lauterbur were awarded the 2003 Nobel Prize in Physiology or Medicine for their "discoveries concerning magnetic resonance imaging".
all persons who were members of the Southern Sudan Legislative Assembly; and all South Sudanese who were members of the National Assembly of Sudan, by virtue of their membership in that Assembly. Members of the Council of Ministers who are not members of the National Legislative Assembly must participate in its deliberations but do not have the right to vote. Persons who wish to become members of the National Legislative Assembly must fulfill the eligibility requirements set down by the Constitution for membership of the National Legislature.
=== Molten oxide electrolysis === Molten oxide electrolysis (MOE) uses electrolysis of molten iron oxide to yield metallic iron. It is studied in laboratory-scale experiments and is proposed as a method for industrial iron production that has no direct emissions of carbon dioxide. It uses a liquid iron cathode, an anode formed from an alloy of chromium, aluminium and iron, and the electrolyte is a mixture of molten metal oxides into which iron ore is dissolved. The current keeps the electrolyte molten and reduces the iron oxide. Oxygen gas is produced in addition to liquid iron. The only carbon dioxide emissions come from any fossil fuel-generated electricity used to heat and reduce the metal.
== Epidemiology == Sydenham's chorea is primarily seen in children. As with rheumatic fever, Sydenham's chorea is seen more often in less affluent communities, whether in the developing world or in aboriginal communities in the global North. High rates of impetigo are a marker for widespread streptococcal transmission. In the UK, there are approximately 20 cases per year, according to a BPSU surveillance study.
== History == Antimicrobial use has been common practice for at least 2000 years. Ancient Egyptians and ancient Greeks used specific molds and plant extracts to treat infection. In the 19th century, microbiologists such as Louis Pasteur and Jules Francois Joubert observed antagonism between some bacteria and discussed the merits of controlling these interactions in medicine. Louis Pasteur's work in fermentation and spontaneous generation led to the distinction between anaerobic and aerobic bacteria. The information garnered by Pasteur led Joseph Lister to incorporate antiseptic methods, such as sterilizing surgical tools and debriding wounds into surgical procedures. The implementation of these antiseptic techniques drastically reduced the number of infections and subsequent deaths associated with surgical procedures. Louis Pasteur's work in microbiology also led to the development of many vaccines for life-threatening diseases such as anthrax and rabies. On September 3, 1928, Alexander Fleming returned from a vacation and discovered that a Petri dish filled with Staphylococcus was separated into colonies due to the antimicrobial fungus Penicillium rubens. Fleming and his associates struggled to isolate the antimicrobial but referenced its therapeutic potential in 1929 in the British Journal of Experimental Pathology. In 1942, Howard Florey, Ernst Chain, and Edward Abraham used Fleming's work to purify and extract penicillin for medicinal uses earning them the 1945 Nobel Prize in Medicine.
Sources: en.wikipedia.org
Native GLP-1 is a short-lived peptide cleared within one to two minutes by dipeptidyl peptidase-4 and related enzymes. Semaglutide keeps the receptor-binding backbone but adds substitutions and a lipid chain. These changes block the main cleavage site and allow reversible albumin binding, extending the half-life to roughly 165 hours.
Albumin is the most abundant protein in plasma and carries molecules that bear fatty-acid chains. Binding shields the peptide from renal filtration and from peptidases, keeping a circulating reservoir. Slow release from this reservoir produces sustained receptor occupancy and supports infrequent dosing.
The insulinotropic effect is glucose-dependent, meaning secretion increases mainly when glucose is elevated. This property is often described as lowering the chance of hypoglycaemia when the compound is used alone. Other glucose-lowering agents used at the same time can still cause low blood glucose.
It belongs to the incretin mimetic class and acts as a long-acting glucagon-like peptide-1 receptor agonist. The class includes several peptides with different half-lives and routes of administration.