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Hemin
Hemin (haemin; ferric chloride heme) is an iron-containing porphyrin with chlorine that can be formed from a heme group, such as heme B found in the hemoglobin of human blood. Chemistry Hemin is protoporphyrin IX containing a ferric iron (Fe3+) ion with a coordinating chloride ligand. Chemically, hemin differs from the related heme-compound hematin chiefly in that the coordinating ion is a chloride ion in hemin, whereas the coordinating ion is a hydroxide ion in hematin. The iron ion in haem is ferrous (Fe2+), whereas it is ferric (Fe3+) in both hemin and hematin. Hemin is endogenously produced in the human body, for example during the turnover of old red blood cells. It can form inappropriately as a result of hemolysis or vascular injury. Several proteins in human blood bind to hemin, such as hemopexin and serum albumin. Pharmacological use A lyophilised form of hemin is used as a pharmacological agent in certain cases for the treatment of porphyria attacks, particularl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aminolevulinic Acid Synthase
Aminolevulinic acid synthase (ALA synthase, ALAS, or delta-aminolevulinic acid synthase) is an enzyme () that catalyzes the synthesis of δ-aminolevulinic acid (ALA) the first common precursor in the biosynthesis of all tetrapyrroles such as hemes, cobalamins and chlorophylls. The reaction is as follows: :succinyl-CoA + glycine \rightleftharpoons δ-aminolevulinic acid + CoA + CO2 This enzyme is expressed in all non-plant eukaryotes and the α-class of proteobacteria and the reaction it catalyses is sometimes referred to as the Shemin pathway for ALA formation. Other organisms produce ALA through a three enzyme pathway known as the C5 pathway. ALA is synthesized through the condensation of glycine and succinyl-CoA. In humans, transcription of ALA synthase is tightly controlled by the presence of Fe2+-binding elements, to prevent accumulation of porphyrin intermediates in the absence of iron. There are two forms of ALA synthase in the body. One form is expressed in red blood cell ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carbon Monoxide-releasing Molecules
Carbon monoxide-releasing molecules (CORMs) are chemical compounds designed to release controlled amounts of carbon monoxide (CO). CORMs are being developed as potential therapeutic agents to locally deliver CO to cells and tissues, thus overcoming limitations of CO gas inhalation protocols. CO is best known for its toxicity in carbon monoxide poisoning at high doses. However, CO is a gasotransmitter and supplemental low dosage of CO has been linked to therapeutic benefits. Pre-clinical research has focused on CO's anti-inflammatory activity with significant applications in cardiovascular disease, oncology, transplant surgery, and neuroprotection. History The simplest source of CO is from a combustion reaction via burning sources such as fossil fuels or fire wood. Sources releasing CO upon thermal decomposition or combustion are generally not considered CORMs. Therapeutic interest in CO dates back to the study of factitious airs (hydrocarbonate) in the 1790s by Thomas Beddoes ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heme
Heme, or haem (pronounced / hi:m/ ), is a precursor to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver. In biochemical terms, heme is a coordination complex "consisting of an iron ion coordinated to a porphyrin acting as a tetradentate ligand, and to one or two axial ligands." The definition is loose, and many depictions omit the axial ligands. Among the metalloporphyrins deployed by metalloproteins as prosthetic groups, heme is one of the most widely used and defines a family of proteins known as hemoproteins. Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase. The word ''haem'' is derived from Greek ''haima'' meaning "blood". Function Hemoproteins have diverse biological functions incl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heme Oxygenase
Heme oxygenase, or haem oxygenase, (HMOX, commonly abbreviated as HO) is an enzyme that catalyzes the degradation of heme to produce biliverdin, ferrous ion, and carbon monoxide. There are many heme degrading enzymes in nature. In general, only aerobic heme degrading enzymes are referred to as HMOX-like enzymes whereas anaerobic enzymes are typically not affiliated with the HMOX family. Heme oxygenase Heme oxygenase (alternatively spelled using haem or oxidase) catalyzes the degradation of heme to biliverdin/bilirubin, ferrous ion, and carbon monoxide. The human genome may encode three isoforms of HMOX. The degradation of heme forms three distinct chromogens as seen in healing cycle of a bruise. This reaction can occur in virtually every cell and platelet; the classic example is the healing process of a contusion, which forms different chromogens as it gradually heals: (red) heme to (green) biliverdin to (yellow) bilirubin which is widely known for jaundice. In general, aside ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Haemophilus Influenzae
''Haemophilus influenzae'' (formerly called Pfeiffer's bacillus or ''Bacillus influenzae'') is a Gram-negative, non-motile, coccobacillary, facultatively anaerobic, capnophilic pathogenic bacterium of the family Pasteurellaceae. The bacteria are mesophilic and grow best at temperatures between 35 and 37℃. ''H. influenzae'' was first described in 1892 by Richard Pfeiffer during an influenza pandemic when he incorrectly described ''Haemophilus influenzae'' as the causative microbe, which is why the bacteria retain the name "influenza". ''H. influenzae'' is responsible for a wide range of localized and invasive infections, typically in infants and children, including pneumonia, meningitis, or bloodstream infections. Treatment consists of antibiotics, however ''H. influenzae'' is often resistant to the penicillin family but augmentin can be used in mild cases. The recommended form of prevention is a series of the Hib vaccine and boosters, which are most often given under the ag ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemolysis
Hemolysis or haemolysis (), also known by several other names, is the rupturing (lysis) of red blood cells (erythrocytes) and the release of their contents (cytoplasm) into surrounding fluid (e.g. blood plasma). Hemolysis may occur in vivo or in vitro. One cause of hemolysis is the action of hemolysins, toxins that are produced by certain pathogenic bacteria or fungi. Another cause is intense physical exercise. Hemolysins damage the red blood cell's cytoplasmic membrane, causing lysis and eventually cell death. Etymology From hemo- + -lysis, from , "blood") + , "loosening"). Inside the body Hemolysis inside the body can be caused by a large number of medical conditions, including some parasites (''e.g.'', ''Plasmodium''), some autoimmune disorders (''e.g.'', autoimmune haemolytic anaemia, drug-induced hemolytic anemia, atypical hemolytic uremic syndrome (aHUS)), some genetic disorders (''e.g.'', Sickle-cell disease or G6PD deficiency), or blood with too low a solute conc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Haematin
Haematin (also known as hematin, ferriheme, hematosin, hydroxyhemin, oxyheme, phenodin, or oxyhemochromogen) is a dark bluish or brownish pigment containing iron in the ferric state, obtained by the oxidation of haem. Haematin inhibits the synthesis of porphyrin, and stimulates the synthesis of globin. It is a component of cytochromes and peroxidases Peroxidases or peroxide reductases ( EC numberbr>1.11.1.x are a large group of enzymes which play a role in various biological processes. They are named after the fact that they commonly break up peroxides. Functionality Peroxidases typically ca ..., and is also used as a reagent. References Iron(III) compounds Pigments {{organic-compound-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protoporphyrin IX
Protoporphyrin IX is an organic compound, classified as a porphyrin, that plays an important role in living organisms as a precursor to other critical compounds like heme (hemoglobin) and chlorophyll. It is a deeply colored solid that is not soluble in water. The name is often abbreviated as PPIX. Protoporphyrin IX contains a porphine core, a tetrapyrrole macrocycle with a marked aromatic character. Protoporphyrin IX is essentially planar, except for the N-H bonds that are bent out of the plane of the rings, in opposite (trans) directions. Nomenclature The general term protoporphyrin refers to porphine derivatives that have the outer hydrogen atoms in the four pyrrole rings replaced by other functional groups. The prefix proto often means 'first' in science nomenclature (such as carbon protoxide), hence Hans Fischer is thought to have coined the name protoporphyrin as the first class of porphyrins. Fischer described iron-deprived heme becoming the "proto-" porphyrin, particu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemopexin
Hemopexin (or haemopexin; Hpx; Hx), also known as beta-1B-glycoprotein, is a glycoprotein that in humans is encoded by the ''HPX'' gene and belongs to the hemopexin family of proteins. Hemopexin is the plasma protein with the highest binding affinity for heme. Hemoglobin ''itself'' circulating ''alone'' in the blood plasma (called ''free hemoglobin'', as opposed to the hemoglobin situated in and circulating with the red blood cell.) will soon be oxidized into met-hemoglobin which then further disassociates into ''free'' heme along with globin chain. The free heme will then be oxidized into free met-heme and sooner or later the hemopexin will come to bind free met-heme together, forming a complex of met-heme and hemopexin, continuing their journey in the circulation until reaching a receptor, such as CD91, on hepatocytes or macrophages within the spleen, liver and bone marrow. Hemopexin's arrival and subsequent binding to the free heme not only prevent heme's pro-oxidant and pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hematin
Haematin (also known as hematin, ferriheme, hematosin, hydroxyhemin, oxyheme, phenodin, or oxyhemochromogen) is a dark bluish or brownish pigment containing iron in the ferric state, obtained by the oxidation of haem. Haematin inhibits the synthesis of porphyrin, and stimulates the synthesis of globin. It is a component of cytochromes Cytochromes are redox-active proteins containing a heme, with a central Fe atom at its core, as a cofactor. They are involved in electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of bi ... and peroxidases, and is also used as a reagent. References Iron(III) compounds Pigments {{organic-compound-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Intravenous Therapy
Intravenous therapy (abbreviated as IV therapy) is a medical technique that administers fluids, medications and nutrients directly into a person's vein. The intravenous route of administration is commonly used for rehydration or to provide nutrients for those who cannot, or will not—due to reduced mental states or otherwise—consume food or water by mouth. It may also be used to administer medications or other medical therapy such as blood products or electrolytes to correct electrolyte imbalances. Attempts at providing intravenous therapy have been recorded as early as the 1400s, but the practice did not become widespread until the 1900s after the development of techniques for safe, effective use. The intravenous route is the fastest way to deliver medications and fluid replacement throughout the body as they are introduced directly into the circulatory system and thus quickly distributed. For this reason, the intravenous route of administration is also used for the consump ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ludwik Karol Teichmann
Ludwik Karol Teichmann-Stawiarski (1823–1895) was a Polish anatomist and discoverer of a new way of research in forensic medicine, after whom Teichmann crystals are called. Life Teichmann was born in Lublin. In 1856, Teichmann became a Doctor of Medicine at the University of Göttingen. In 1861, he became a Professor of pathological anatomy at the Jagiellonian University in Kraków. and in 1868 he became a professor of descriptive and comparative anatomy there, where he also served as Rector from 1877 to 1878. He introduced injection and corrosion techniques into pathology and used them to study the lymphatic system in health and disease. He discovered haemin crystals, now known as Teichmann's crystals. Teichmann died on in Kraków. Works Among his works, ''Das saugadersystem vom anatomischen standpunkte'' (1861) in particular acquired recognition. See also *Hemin Hemin (haemin; ferric chloride heme) is an iron-containing porphyrin with chlorine that can be ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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