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1. in surgery, the disruption of tissue by physical means to form an amorphous residuum, as in electrocoagulation or hotocoagulation.
2. in colloid chemistry, solidification of a sol into a gelatinous mass.
blood coagulation clotting.
diffuse intravascular coagulation (disseminated intravascular coagulation (DIC)) see disseminated intravascular coagulation.
coagulation factors factors essential to normal blood clotting, whose absence, diminution, or excess may lead to abnormality of the clotting. Twelve factors, commonly designated by Roman numerals, have been described (I–V and VII–XIII; VI is no longer considered to have a clotting function). (See table 6.)

Factor I is a high-molecular-weight plasma protein that is converted to fibrin through the action of thrombin; deficiency conditions are called afibrinogenemia and hypofibrinogenemia. Called also fibrinogen. Factor II is a glycoprotein present in the plasma that is converted into thrombin in the common pathway of coagulation; deficiency is called hypoprothrombinemia. Called also prothrombin. Factor III is involved in the extrinsic pathway of coagulation, activating factor X; called also tissue thromboplastin or factor.

Factor IV is calcium, required in many stages of blood clotting. Factor V is a heat- and storage-labile material, present in plasma and not in serum and is involved in the intrinsic and extrinsic pathways of coagulation, causing the cleavage of prothrombin to the active thrombin. Deficiency causes parahemophilia. Called also accelerator globulin or factor and proaccelerin. Factor VI is no longer considered in the scheme of hemostasis, and hence is assigned neither a name nor a function.

Factor VII is a heat- and storage-stable material, present in serum and in plasma and participating in the extrinsic pathway of coagulation, acting with factor III to activate factor X. Deficiency, either hereditary or acquired (vitamin k deficiency), leads to hemorrhagic tendency. Called also proconvertin and serum prothrombin conversion accelerator (SPCA). Factor VIII is a relatively storage-labile material that participates in the intrinsic pathway of coagulation, acting as a cofactor in the activation of factor X. Deficiency, an X-linked recessive trait, results in hemophilia a (classical hemophilia). Called also antihemophilic factor (AHF) and antihemophilic globulin (AHG). Factor IX is a relatively storage-stable substance involved in the intrinsic pathway of coagulation, acting to activate factor X. Deficiency of this factor results in a hemorrhagic syndrome called hemophilia b (or Christmas disease), which is similar to classical hemophilia A. It is treated with purified preparations of the factor, derived from human plasma or recombinant, or with factor IX complex. Called also plasma thromboplastin component (PTC) and antihemophilic factor B.

Factor X is a heat-labile material with some storage stability, which is involved in both intrinsic and extrinsic pathways of coagulation, uniting them to begin the common pathway. Once activated, it complexes with calcium, phospholipid, and activated factor V to form prothrombinase, which cleaves and activates prothrombin to thrombin. Called also Stuart or Stuart-Prower factor. Factor XI is a stable factor involved in the intrinsic pathway of coagulation, activating factor IX. Deficiency results in hemophilia c. Called also plasma thromboplastin antecedent (PTA) and antihemophilic factor C. Factor XII is a stable factor activated by contact with glass or other foreign substances, which initiates coagulation through the intrinsic pathway by activating factor XI; called also Hageman factor. Factor XIII is a factor that polymerizes fibrin monomers, enabling fibrin to form a firm blood clot. Deficiency causes a clinical hemorrhagic diathesis. Called also fibrin-stabilizing factor.


A group of enzymes that catalyze the calcium-dependent acyl transfer reaction in which the amide moiety of peptide-bound glutaminyl residues serve as acyl donor; a specific transglutaminase covalently cross-links fibrin molecules between glutamine and the ε-amino group of a lysyl residue, thus producing a more stable fibrin clot; another transglutaminase participates in the formation of the chemically resistant envelope of the stratum corneum during terminal differentiation of keratinocytes.


/trans·glu·tam·in·ase/ (trans″gloo-tam´in-ās) an enzyme, formed by cleavage and activation of protransglutaminase, which forms stabilizing covalent bonds within fibrin strands. It is the activated form of coagulation factor XIII.


the activated form of protransglutaminase, which forms stabilizing covalent bonds within fibrin strands; called also coagulation factor XIIIa.
References in periodicals archive ?
In particular, transglutaminases (TG) can offer the possibility to enzymatically cross-linked collagen nanofiber mats by formation of the amide cross-link from [gamma]-carboxamide and primary amine functionalities [35].
Dentro dessa classe de enzimas, capazes de "fabricar estrutura", destacam-se as transglutaminases, sobretudo as produzidas a partir de microrganismo, as MTGases (WEISS et al.
The SC is made up of corneocytes: terminally differentiated keratinocytes, highly cross-linked by transglutaminases with cornified envelope proteins such as loricrin, involucrin, filaggrin, and small proline-rich proteins.
36) The protein Hwplp is a substrate for host transglutaminases and thus it can be covalently cross linked to the surface of host tissue and result in adhesion of organism to the host.
The FXIII-A, a protransglutaminase enzyme, belongs to the family of transglutaminases.
Transglutaminases play a key role in the pathogenesis of gluten intolerance.
Most clinical labs measure antibodies against transglutaminase 2, but not against other transglutaminases.
I think that there's a good chance that we will find a compound because there are many existing compounds that inhibit other transglutaminases.
arabinanases, endoglucanases, galactanases, glycosidases, xylanases, oxidases, proteases peptidases, phospholipases, lactases, transglutaminases Animal feed: enzymes are used to Phytases, [beta]-glucanases, enhance digestion and nutritional xylanases, galactanases, content of animal feed.
Dartmouth College (Hanover, NH) has patented a method for preventing the infection of a mammalian host by a microorganism through the administration of substrates for transglutaminases or antibodies against such substrates that inhibit the transglutaminase-mediated interaction of the microorganism with the mammalian host.
Roberto Chica from the laboratories of Jeffrey Keillor, MCIC, and Joelle Pelletier, MCIC, at the Universite de Montreal described the development of mutant transglutaminases that could catalyze peptide bond formation between a variety of amino acid derivatives.
Mehta (experimental therapeutics, University of Texas) and Eckert (Case School of Medicine) provide information on the biological relevance of transglutaminases in cancer, inflammation, autoimmune diseases, and other related areas of research.