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Staphylokinase
Staphylokinase (SAK; also known as staphylococcal fibrinolysin or Müller's factor) is a protein produced by ''Staphylococcus aureus''. It contains 136 amino acid residues and has a molecular mass of 15kDa. Synthesis of staphylokinase occurs in late exponential phase. It is similar to streptokinase. Staphylokinase is positively regulated by the "agr" gene regulator. It activates plasminogen to form plasmin, which digests fibrin clots. This disrupts the fibrin meshwork which forms to keep infections localized. Staphylokinase interacts with plasminogen to form a 1:1 complex that exposes the active site of the plasminogen molecule. The plasmin Sak complex is neutralized by α2- antiplasmin in plasma in the absence of fibrin, resulting in lysis. However, in the presence of fibrin, the inhibition is delayed, creating a unique mechanism for fibrin selectivity in plasma. Staphylokinase also cleaves IgG and complement component C3b, inhibiting phagocytosis. Structure The full length of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Streptokinase
Streptokinase is a thrombolysis, thrombolytic medication activating plasminogen by nonenzymatic mechanism. As a medication it is used to thrombolysis, break down clots in some cases of myocardial infarction (heart attack), pulmonary embolism, and arterial thromboembolism. The type of heart attack it is used in is an Myocardial infarction#STEMI, ST elevation myocardial infarction (STEMI). It is given by intravenous, injection into a vein. Side effects include nausea, bleeding, low blood pressure, and allergic reactions. A second use in a person's lifetime is not recommended. While no harm has been found with use in pregnancy, it has not been well studied in this group. Streptokinase is in the antithrombotic family of medications and works by turning on the fibrinolytic system. Streptokinase was discovered in 1933 from beta-hemolytic streptococci. It is on the WHO Model List of Essential Medicines, World Health Organization's List of Essential Medicines. It is no longer commerc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Staphylococcus Aureus
''Staphylococcus aureus'' is a Gram-positive spherically shaped bacterium, a member of the Bacillota, and is a usual member of the microbiota of the body, frequently found in the upper respiratory tract and on the skin. It is often positive for catalase and nitrate reduction and is a facultative anaerobe, meaning that it can grow without oxygen. Although ''S. aureus'' usually acts as a commensal of the human microbiota, it can also become an opportunistic pathogen, being a common cause of skin infections including abscesses, respiratory infections such as sinusitis, and food poisoning. Pathogenic strains often promote infections by producing virulence factors such as potent protein toxins, and the expression of a cell-surface protein that binds and inactivates antibodies. ''S. aureus'' is one of the leading pathogens for deaths associated with antimicrobial resistance and the emergence of antibiotic-resistant strains, such as methicillin-resistant ''S. aur ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibrinolysin
Fibrinolysin is an enzyme derived from plasma of bovine origin (plasmin) or extracted from cultures of certain bacteria. It is used locally only and exclusively together with the enzyme desoxyribonuclease (extracted from bovine pancreas). Fibrinolysin and desoxyribonuclease both act as lytic enzymes. The combination is available as ointment containing 1 BU (Biological unit, Biological Unit) fibrinolysin and 666 BUs desoxyribonuclease per gram. Fibrinolysin attacks and inactivates fibrin molecules occurring in undesirable exudates on the surface of the human body and on human mucosa, e.g., in superficial wounds and Burn (injury), burns, while desoxyribonuclease targets and destroys (human) DNA. The combination of the two enzymes has a synergistic effect on necrotic but not on living biological tissue, tissue. According to the manufacturer the ointment provides enhanced wound cleaning and accelerates the healing process. Both enzymes are marginally resorbed into systemic circulation ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Silent Mutation
Silent mutations, also called synonymous or samesense mutations, are mutations in DNA that do not have an observable effect on the organism's phenotype. The phrase ''silent mutation'' is often used interchangeably with the phrase '' synonymous mutation''; however, synonymous mutations are not always silent, nor vice versa. Synonymous mutations can affect transcription, splicing, mRNA transport, and translation, any of which could alter phenotype, rendering the synonymous mutation non-silent. The substrate specificity of the tRNA to the rare codon can affect the timing of translation, and in turn the co-translational folding of the protein. This is reflected in the codon usage bias that is observed in many species. Mutations that cause the altered codon to produce an amino acid with similar functionality (''e.g.'' a mutation producing leucine instead of isoleucine) are often classified as silent; if the properties of the amino acid are conserved, this mutation does not usually s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EC 3
EC3 can refer to: People * Ethan Carter III (EC3) (born 1983), American professional wrestler Places * EC3, a district in the London EC postcode area Groups, organizations, companies * European Cybercrime Centre * EarthCheck, formerly EC3 Global; international tourism advisory group Transportation * BJEV ''EC3'', a Chinese electric vehicle * KUR ''EC3 class'', a class of steam locomotive * EC-3 radar, Italian WWII radar Other uses * Dolby Digital Plus, also known as EC-3 * Hydrolase enzymes (EC 3); see List of EC numbers (EC 3) See also * ECCC (other) {{Letter-NumberCombDisambig ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibrinolysin
Fibrinolysin is an enzyme derived from plasma of bovine origin (plasmin) or extracted from cultures of certain bacteria. It is used locally only and exclusively together with the enzyme desoxyribonuclease (extracted from bovine pancreas). Fibrinolysin and desoxyribonuclease both act as lytic enzymes. The combination is available as ointment containing 1 BU (Biological unit, Biological Unit) fibrinolysin and 666 BUs desoxyribonuclease per gram. Fibrinolysin attacks and inactivates fibrin molecules occurring in undesirable exudates on the surface of the human body and on human mucosa, e.g., in superficial wounds and Burn (injury), burns, while desoxyribonuclease targets and destroys (human) DNA. The combination of the two enzymes has a synergistic effect on necrotic but not on living biological tissue, tissue. According to the manufacturer the ointment provides enhanced wound cleaning and accelerates the healing process. Both enzymes are marginally resorbed into systemic circulation ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dumbbell
The dumbbell, a type of free weight, is a piece of equipment used in weight training. It is usually used individually and/or in pairs, with one in each hand. History The forerunner of the dumbbell, halteres, were used in ancient Greece as lifting weights and also as weights for the ancient Greek version of the long jump. A kind of dumbbell was also used in India for more than a millennium, shaped like a club – so it was named Indian club. The design of the "Meel", as the club was referred to, can be seen as a halfway point between a barbell and a dumbbell. It was generally used in pairs, in workouts by wrestlers, bodybuilders, sports players, and others wishing to increase strength and muscle size. Etymology The term "dumbbell" or "dumb bell" or "dumb-bell" originated in late Stuart England. In 1711 the poet Joseph Addison mentioned exercising with a "dumb bell" in an essay published in ''The Spectator''. Although Addison elsewhere in the same publication describes havin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's Peptide, polypeptide chain that is self-stabilizing and that Protein folding, folds independently from the rest. Each domain forms a compact folded Protein tertiary structure, three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or Disulfide bond, disulfide bridges. Domains often form functional units, such as the calcium-binding EF-hand, EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimera (protein), chimeric ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Histidine
Histidine (symbol His or H) is an essential amino acid that is used in the biosynthesis of proteins. It contains an Amine, α-amino group (which is in the protonated –NH3+ form under Physiological condition, biological conditions), a carboxylic acid group (which is in the deprotonated –COO− form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a positively charged amino acid at physiological pH. Initially thought essential amino acid, essential only for infants, it has now been shown in longer-term studies to be essential for adults also. It is Genetic code, encoded by the Genetic code, codons CAU and CAC. Histidine was first isolated by Albrecht Kossel and Sven Gustaf Hedin in 1896. The name stems from its discovery in tissue, from ''histós'' "tissue". It is also a Precursor (chemistry), precursor to histamine, a vital inflammatory agent in immune responses. The acyl radical (chemistry), radical is histidyl. Pro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Arginine
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidinium, guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the -arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is Genetic code, encoded by the DNA codon table, codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the Precursor (chemistry), precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid. The one-letter symbol R was assigned to arginine for its phonetic similarity. History Arginine was first isolated in 1886 from Lupinus luteus, yellow lupin seedlings by the German chemist Ernst Schulze (chemist), Ernst Schulze and his assistant Ernst Steiger. He named it from the Greek ''árg ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycine
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine disrupts the formation of alpha-helices in secondary protein structure. Its small side chain causes it to favor random coils instead. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a '' Clostridium tetani'' infection) can cause spastic paralysis due to uninhibited muscle contraction. It is the only achiral proteinogenic amino acid. It can fit into both hydrophilic and hydrophobic environments, due to its minimal side chain of only one hydrogen atom. History and etymology Glycine was discovered in 1820 by French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid. He originally called it "sugar of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Serine
Serine (symbol Ser or S) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α- amino group (which is in the protonated − form under biological conditions), a carboxyl group (which is in the deprotonated − form under biological conditions), and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC. Occurrence This compound is one of the proteinogenic amino acids. Only the L- stereoisomer appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865 by Emil Cramer. Its name is derived from the Latin for silk, '' sericum''. Serine's structure was established in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
