|
Batroxobin
Batroxobin, also known as reptilase, is a snake venom enzyme with Venombin A activity produced by ''Bothrops atrox'' and ''Bothrops moojeni'', venomous species of pit viper found east of the Andes in South America. It is a hemotoxin which acts as a serine protease similarly to thrombin, and has been the subject of many medical studies as a replacement of thrombin. Different enzymes, isolated from different species of ''Bothrops'', have been called batroxobin, but unless stated otherwise, this article covers the batroxobin produced by ''B. moojeni'', as this is the most studied variety. History Bothrops atrox was described by Carl Linnaeus as early as 1758, but batroxobin, the active compound in its venom, was first described only in 1954 by H. Bruck and G. Salem. In the years following, this first description of batroxobin was shown to have several uses in surgery. Because of the increasing interest in the properties of batroxobin, several studies on its hemostatic effect and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thrombin Time
The thrombin time (TT), also known as the thrombin clotting time (TCT), is a blood test that measures the time it takes for a clot to form in the plasma of a blood sample containing anticoagulant, after an excess of thrombin has been added. It is used to diagnose blood coagulation disorders and to assess the effectiveness of fibrinolytic therapy. This test is repeated with pooled plasma from normal patients. The difference in time between the test and the 'normal' indicates an abnormality in the conversion of fibrinogen (a soluble protein) to fibrin, an insoluble protein. The thrombin time compares the rate of clot formation to that of a sample of normal pooled plasma. Thrombin is added to the samples of plasma. If the time it takes for the plasma to clot is prolonged, a quantitative (fibrinogen deficiency) or qualitative (dysfunctional fibrinogen) defect is present. In blood samples containing heparin, a substance derived from snake venom called batroxobin (formerly reptilase) is ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ancrod
Ancrod (current brand name: Viprinex) is a defibrinogenating agent derived from the venom of the Malayan pit viper. Defibrinogenating blood produces an anticoagulant effect. Ancrod is not approved or marketed in any country. It is a thrombin-like serine protease. Medical use As of 2017 ancrod was not marketed for any medical use. Pregnancy Category X : Ancrod was not found to be teratogenic in animal studies, but some fetal deaths occurred as a result of placental hemorrhages in animals given high doses; therefore, it should not be used during pregnancy as the defibrinogenation mechanism of ancrod might be expected to interfere with the normal implantation of the fertilized egg. Contraindications and precautions * Known bleeding disorders of any origin or any unexplained excessive bleedings in the past. * Platelet counts of less than 100,000 (even if asymptomatic), exemption : HIT (Heparin- induced thrombocytopenia). * Planned surgery or short before delivery. * Active ulcera ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Venombin A
Venombin A (, ''alpha-fibrinogenase'', ''habutobin'', ''zinc metalloproteinase Cbfib1.1'', ''zinc metalloproteinase Cbfib1.2'', ''zinc metalloproteinase Cbfib2'', ''ancrod'') is an enzyme. This enzyme catalyses the following chemical reaction : Selective cleavage of Arg- bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme This enzyme is a thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group. Examples include ancrod and batroxobin, two serine proteases from snakes that have been used in medical preparations. Applications Venombin A enzymes are the sole representatives of the defibrinogenating agent class of drugs, which by its protease action removes fibrinogen from the circulation. They are thought to act as an antithrombotic by depletion of fibrinogen. They are different from thrombin in that they only cleave fibrinogen alpha chain (those do cleave b ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Defibrinogenating Agent
Venombin A (, ''alpha-fibrinogenase'', ''habutobin'', ''zinc metalloproteinase Cbfib1.1'', ''zinc metalloproteinase Cbfib1.2'', ''zinc metalloproteinase Cbfib2'', ''ancrod'') is an enzyme. This enzyme catalyses the following chemical reaction : Selective cleavage of Arg- bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme This enzyme is a thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group. Examples include ancrod and batroxobin, two serine proteases from snakes that have been used in medical preparations. Applications Venombin A enzymes are the sole representatives of the defibrinogenating agent class of drugs, which by its protease action removes fibrinogen from the circulation. They are thought to act as an antithrombotic by depletion of fibrinogen. They are different from thrombin in that they only cleave fibrinogen alpha chain (those do cleave b ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibrinopeptide B
The fibrinopeptides, fibrinopeptide A (FpA) and fibrinopeptide B (FpB), are peptides which are located in the central region of the fibrous glycoprotein fibrinogen (factor I) and are cleaved by the enzyme thrombin (factor IIa) to convert fibrinogen into covalently-linked fibrin (factor IA) monomers. The N-terminal FpA is cleaved from the Aα chains of fibrinogen and FpB from the Bβ chains of fibrinogen, with FpA released before FpB. Subsequent to their formation, fibrin monomers are converted to cross-linked fibrin polymers by the action of thrombin-activated factor XIII (fibrin stabilizing factor), and these fibrin polymers form the backbone of a thrombus (blood clot). Hence, the fibrinopeptides are sensitive markers of fibrinogenesis (fibrin generation), thrombin activity, and coagulation. FpA is a 16-amino acid peptide. The half-life of FpA is very short at approximately 3 to 5 minutes. Hence, FpA levels provide a relatively transient measure of coagulation activati ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibrinopeptide A
The fibrinopeptides, fibrinopeptide A (FpA) and fibrinopeptide B (FpB), are peptides which are located in the central region of the fibrous glycoprotein fibrinogen (factor I) and are cleaved by the enzyme thrombin (factor IIa) to convert fibrinogen into covalently-linked fibrin (factor IA) monomers. The N-terminal FpA is cleaved from the Aα chains of fibrinogen and FpB from the Bβ chains of fibrinogen, with FpA released before FpB. Subsequent to their formation, fibrin monomers are converted to cross-linked fibrin polymers by the action of thrombin-activated factor XIII (fibrin stabilizing factor), and these fibrin polymers form the backbone of a thrombus (blood clot). Hence, the fibrinopeptides are sensitive markers of fibrinogenesis (fibrin generation), thrombin activity, and coagulation. FpA is a 16-amino acid peptide. The half-life of FpA is very short at approximately 3 to 5 minutes. Hence, FpA levels provide a relatively transient measure of coagulation activ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pichia Pastoris
''Pichia pastoris'' is a species of methylotrophic yeast. It was found in the 1960s, with its feature of using methanol as a source of carbon and energy. After years of study, ''P. pastoris'' was widely used in biochemical research and biotech industries. With strong potential for being an expression system for protein production, as well as being a model organism for genetic study, ''P. pastoris'' has become important for biological research and biotech applications. In the last decade, some reports reassigned ''P. pastoris'' to the genus ''Komagataella'' with phylogenetic analysis, by genome sequencing of ''P. pastoris''. The genus was split into ''K. phaffii'', ''K. pastoris'', and ''K. pseudopastoris''. ''P. pastoris'' in nature Natural habitat In nature, ''P. pastoris'' is found on trees, such as chestnut trees. They are heterotrophs and they can use several carbon sources for living, like glucose, glycerol and methanol. However, they cannot use lactose. Reproduction ' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Coagulation
Coagulation, also known as clotting, is the process by which blood changes from a liquid to a gel, forming a blood clot. It potentially results in hemostasis, the cessation of blood loss from a damaged vessel, followed by repair. The mechanism of coagulation involves activation, adhesion and aggregation of platelets, as well as deposition and maturation of fibrin. Coagulation begins almost instantly after an injury to the endothelium lining a blood vessel. Exposure of blood to the subendothelial space initiates two processes: changes in platelets, and the exposure of subendothelial tissue factor to plasma factor VII, which ultimately leads to cross-linked fibrin formation. Platelets immediately form a plug at the site of injury; this is called ''primary hemostasis. Secondary hemostasis'' occurs simultaneously: additional coagulation (clotting) factors beyond factor VII ( listed below) respond in a cascade to form fibrin strands, which strengthen the platelet plug. Disorders of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemostatic Effec
An antihemorrhagic (antihæmorrhagic) agent is a substance that promotes hemostasis (stops bleeding). It may also be known as a hemostatic (also spelled haemostatic) agent. Antihemorrhagic agents used in medicine have various mechanisms of action: * Systemic drugs work by inhibiting fibrinolysis or promoting coagulation. * Locally acting hemostatic agents work by causing vasoconstriction or promoting platelet aggregation. Medical uses Hemostatic agents are used during surgical procedures to achieve hemostasis and are categorized as hemostats, sealants and adhesives. They vary based on their mechanism of action, composition, ease of application, adherence to tissue, immunogenicity and cost. These agents permit rapid hemostasis, better visualization of the surgical area, shorter operative times, decreased requirement for transfusions, decreased wound healing time and overall improvement in patient recovery time. Types Systemic There are several classes of antihemorrhagic drug ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Snake Venom
Snake venom is a highly toxic saliva containing zootoxins that facilitates in the immobilization and digestion of prey. This also provides defense against threats. Snake venom is injected by unique fangs during a bite, whereas some species are also able to spit venom. The glands that secrete zootoxins are a modification of the parotid salivary glands found in other vertebrates and are usually located on each side of the head, below and behind the eye, and enclosed in a muscular sheath. The venom is stored in large glands called alveoli in which it's stored before being conveyed by a duct to the base of channeled or tubular fangs through which it's ejected. Venom contains more than 20 different compounds, which are mostly proteins and polypeptides. The complex mixture of proteins, enzymes, and various other substances has toxic and lethal properties. Venom serves to immobilize prey. Enzymes in venom play an important role in the digestion of prey, and various other substances ar ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carl Linnaeus
Carl Linnaeus (; 23 May 1707 – 10 January 1778), also known after his ennoblement in 1761 as Carl von Linné Blunt (2004), p. 171. (), was a Swedish botanist, zoologist, taxonomist, and physician who formalised binomial nomenclature, the modern system of naming organisms. He is known as the "father of modern taxonomy". Many of his writings were in Latin; his name is rendered in Latin as and, after his 1761 ennoblement, as . Linnaeus was born in Råshult, the countryside of Småland, in southern Sweden. He received most of his higher education at Uppsala University and began giving lectures in botany there in 1730. He lived abroad between 1735 and 1738, where he studied and also published the first edition of his ' in the Netherlands. He then returned to Sweden where he became professor of medicine and botany at Uppsala. In the 1740s, he was sent on several journeys through Sweden to find and classify plants and animals. In the 1750s and 1760s, he continued to collect an ... [...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] |
