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Nattokinase
Nattokinase (pronounced ) is an enzyme extracted and purified from a Japanese food called nattō. Nattō is produced by fermentation by adding the bacterium '' Bacillus natto'', which also produces the enzyme, to boiled soybeans. While other soy foods contain enzymes, it is only the nattō preparation that contains the specific nattokinase enzyme. In spite of its name, nattokinase is not a kinase enzyme (and should not be pronounced as such), but a serine protease of the subtilisin family (99.5% identical with ''aprE''). Rather, it is named for the fact that it is an enzyme produced by ''nattōkin'' ( 納豆 菌), the Japanese name for ''Bacillus subtilis '' var ''natto''. When in contact with human blood or blood clots, it exhibits a strong fibrinolytic activity and works by inactivating plasminogen activator inhibitor 1 (PAI-1). Although it should be expected to be digested and inactivated in the human gut like other proteins, a few researchers report that nattokinase is active ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibrinolytic
Fibrinolysis is a process that prevents blood clots from growing and becoming problematic. Primary fibrinolysis is a normal body process, while secondary fibrinolysis is the breakdown of clots due to a medicine, a medical disorder, or some other cause.Dugdale, David et al.Primary or secondary fibrinolysis, Medline Plus. Retrieved 7 August 2011. In fibrinolysis, a fibrin clot, the product of coagulation, is broken down. Its main enzyme plasmin cuts the fibrin mesh at various places, leading to the production of circulating fragments that are cleared by other proteases or by the kidney and liver. Physiology Plasmin is produced in an inactive form, plasminogen, in the liver. Although plasminogen cannot cleave fibrin, it still has an affinity for it, and is incorporated into the clot when it is formed. Tissue plasminogen activator (t-PA) and urokinase are the agents that convert plasminogen to the active plasmin, thus allowing fibrinolysis to occur. t-PA is released into the blood ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proteases (medical And Related Uses)
Proteases (also sometimes referred to as ''proteolytic enzymes'' or ''peptidases'') are in use, or have been proposed or tried, for a number of purposes related to medicine or surgery. Some preparations involving protease have undergone successful clinical trials and have regulatory authorization; and some further ones have shown apparently useful effects in experimental medical studies. Proteases have also been used by proponents of alternative therapies, or identified in materials of traditional or folk medicine. A serine protease of human origin, activated protein C, was produced in recombinant form and marketed as Drotrecogin alfa (also known as Xigris (TM)) and licensed for intensive-care treatment of severe sepsis. It was voluntarily withdrawn by the manufacturer in 2011 after being shown to be ineffective. Some of these uses rely directly on the proteolytic activity: others rely on observations of anti-inflammatory activity. Medical and surgical applications Treatment of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Daiwa Pharmaceutical , a Thoroughbred racehorse
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Daiwa may refer to: Places: *Daiwa, Hiroshima, a former town in Kamo District, Hiroshima, Japan *Daiwa, Shimane, a former village in Ōchi District, Shimane, Japan Companies and related: *Daiwa Securities Group, a Japanese security brokerage *Daiwa House, a Japanese homebuilder *The Daiwa Anglo-Japanese Foundation, a United Kingdom-based charity *Daiwa Adrian Prize, awarded by the Daiwa Anglo-Japanese Foundation *Globeride (formerly Daiwa Seiko Corporation), a Japanese producer of fishing and outdoor equipment *Daiwa Major Daiwa Major ( ja, ダイワメジャー, link=no) is a retired Japanese Thoroughbred racehorse and active sire. A horse who excelled at distances of , he won the Satsuki Shō, the first leg of the Japanese Triple Crown in 2004. His greatest succ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Genetic Engineering
Genetic engineering, also called genetic modification or genetic manipulation, is the modification and manipulation of an organism's genes using technology. It is a set of technologies used to change the genetic makeup of cells, including the transfer of genes within and across species boundaries to produce improved or novel organisms. New DNA is obtained by either isolating and copying the genetic material of interest using recombinant DNA methods or by artificially synthesising the DNA. A construct is usually created and used to insert this DNA into the host organism. The first recombinant DNA molecule was made by Paul Berg in 1972 by combining DNA from the monkey virus SV40 with the lambda virus. As well as inserting genes, the process can be used to remove, or "knock out", genes. The new DNA can be inserted randomly, or targeted to a specific part of the genome. An organism that is generated through genetic engineering is considered to be genetically modified (GM) an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Plasminogen Activator Inhibitor-1
Plasminogen activator inhibitor-1 (PAI-1) also known as endothelial plasminogen activator inhibitor or serpin E1 is a protein that in humans is encoded by the ''SERPINE1'' gene. Elevated PAI-1 is a risk factor for thrombosis and atherosclerosis PAI-1 is a serine protease inhibitor (serpin) that functions as the principal inhibitor of tissue plasminogen activator (tPA) and urokinase (uPA), the activators of plasminogen and hence fibrinolysis (the physiological breakdown of blood clots). It is a serine protease inhibitor (serpin) protein (SERPINE1). The other PAI, plasminogen activator inhibitor-2 (PAI-2) is secreted by the placenta and only present in significant amounts during pregnancy. In addition, protease nexin acts as an inhibitor of tPA and urokinase. PAI-1, however, is the main inhibitor of the plasminogen activators. Genetics The PAI-1 gene is ''SERPINE1'', located on chromosome 7 (7q21.3-q22). There is a common polymorphism known as 4G/5G in the promoter region. The 5G ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Japanese Food
Japanese cuisine encompasses the regional and traditional foods of Japan, which have developed through centuries of political, economic, and social changes. The traditional cuisine of Japan (Japanese: ) is based on rice with miso soup and other dishes; there is an emphasis on seasonal ingredients. Side dishes often consist of fish, pickled vegetables, and vegetables cooked in broth. Seafood is common, often grilled, but also served raw as sashimi or in sushi. Seafood and vegetables are also deep-fried in a light batter, as '. Apart from rice, a staple includes noodles, such as soba and udon. Japan also has many simmered dishes, such as fish products in broth called , or beef in and . Historically influenced by Chinese cuisine, Japanese cuisine has also opened up to influence from Western cuisines in the modern era. Dishes inspired by foreign food—in particular Chinese food—like ramen and , as well as foods like spaghetti, curry and hamburgers, have been adapted to Japanese ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Subtilisin
Subtilisin is a protease (a protein-digesting enzyme) initially obtained from ''Bacillus subtilis''. Subtilisins belong to subtilases, a group of serine proteases that – like all serine proteases – initiate the nucleophilic attack on the peptide (amide) bond through a serine residue at the active site. Subtilisins typically have molecular weights 27kDa. They can be obtained from certain types of soil bacteria, for example, ''Bacillus amyloliquefaciens'' from which they are secreted in large amounts. Nomenclature Subtilisin is also commercially known as ''Alcalase®'', ''Endocut-02L'', ''ALK-enzyme'', ''bacillopeptidase'', ''Bacillus subtilis alkaline proteinase bioprase'', ''bioprase AL'', ''colistinase'', ''genenase I'', ''Esperase®'', ''maxatase'', ''protease XXVII'', ''thermoase'', ''superase'', ''subtilisin DY'', ''subtilopeptidase'', ''SP 266'', ''Savinase®'', ''kazusase'', ''protease VIII'', ''protin A 3L'', ''Savinase®'', ''orientase 10B'', ''protease S.'' It ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Serine Protease
Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. Classification The MEROPS protease classification system counts 16 superfamilies (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority belong to the S1 family of the PA clan (superfamily) of proteases. For superfamilies, P: superfamily, containing a mixture of nucleophile class families, S: purely serine proteases. superfamily. Within each superfamily, families are designated by their catalytic nucleophile, (S: serine proteases). Substrate specificity Serine ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
