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Fibrin, human

Plasmin, fibrinolysin, a serine protease catalyzing Lys-Xaa and Arg-Xaa bond cleavage similar to that of trypsin. Plasmin is the key protease in blood clot lysis, and its major natural substrates are fibrinogen and fibrin. Human plasmin is derived from plasminogen, and is a two-chain protein consisting of the A or H chain (Mr 65 kDa) and the B or L chain (Mr 27.7 kDa). The active site is located in the B chain. The various molecular forms of plasmin are inactivated by protein inhibitors such as the Kunitz type, serpins, soybean and limabean trypsin inhibitors. The most important, fast-acting inhibitor of plasmin... [Pg.292]

Fibrinopeptides the two pairs of peptides (A and B) cleaved from the /V-termini of the 2a and 2P chains of fibrinogen by thrombin. F. arise by cleavage of Arg-GIy bon so that Arg is the C-terminal end of the F, and Gly is the A/-terminal end of the a and P chains of fibrin. Human FA. is Ala-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-(Gly)3-Val-Arg, and human F.B. is Pyr-Glu-Gly-Val-Asn-Asp-Asn-(Glu)2-Gly-(Phe)2-Ser-Ala-Arg. F.A. ranges in size from 14 amino acids (horse, lizard) to 19 (cattle), and F.B. from 9 (rhesus monkeys) to 21 (cattle, elk and kangaroo). The sequences of the F. have been used to establish a detailed phylogenetic tree for mammals which is very similar to the classical one. The F. have a vasoconstrictive effect which serves to keep the coagulation principles from being removed too quickly from an injury site. [Pg.224]

Keywords— Cartilage tissue engineering, 3D scaffold, fibrin, human amniotic membrane, osteoarthritis. [Pg.841]

Spraggon, G., et al. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 389 455-462, 1997. [Pg.298]

Spotnitz, W.D., Mintz, PD., Avery, N., Bithell, T.C., Kaul, S. and Nolan, S.P, Fibrin glue from stored human plasma An inexpensive and efficient method for local blood bank preparation. Am. Surg., 53, 460-464 (1987). [Pg.1127]

Amino acid substitutions on the native y52 8sKIpeptide, coiled-coil domain of human fibrin were able to stabilize the coiled-coil formation. These substitutions were targeted to the positions that compose the interface between coiled-coil strands while the solvent-exposed residues were left unperturbed. This strategy aimed at reducing the likelihood of immunogenicity for future in vivo apphcafion of these materials. In contrast to PEG block copolymers with end blocks that are not used for directed assembly, PEG copolymers with coiled-coil protein motives aim to enhance intermolecular interactions and control over the assembly conditions [85, 173]. [Pg.158]

This is a dry sponge of human fibrin prepared by elotting a foam of human fibrinogen solution with human thrombin. It is then freeze-dried, cut into shapes and sterilized by dry heat at 130°C for 3 hours. Before use, it is saturated with thrombin solution. Blood coagulation occurs in contact with the thrombin in the interstices of the foam. [Pg.422]

Kudryk B Robinson D., Netre C., et al. Measurement in human blood of fibrinogen/fibrin fragments containing the B beta 15-42 sequence. Thromb Res 1982 25,277-91. [Pg.167]

Such clots—also known as emboli—present a serious hazard by their potential for blocking circulation of blood to vital organs. The considerable research devoted to agents that will lyse the fibrin in clots has led to the development of the clinically useful agent, uj-okinase. This drug is a fibrinolytic proteinaceous enzyme isolated from human urine. The difficulty involved in isolation of significant amounts and the antigenicity of urokinase and a related... [Pg.376]

Yang SH et al (2008) Three-dimensional culture of human nucleus pulposus cells in fibrin clot comparisons on cellular proliferation and matrix synthesis with cells in alginate. Artif Organs 32(l) 70-73... [Pg.230]

The ability of some component of human urine to dissolve fibrin clots was first noted in 1885. It was not until the 1950s, however, that the active substance was isolated and named urokinase. [Pg.350]

Han B, Schwab IR, Madsen TK, Isseroff RR. A fibrin-based bioengineered ocular surface with human corneal epithelial stem cells. Cornea 21 505-510... [Pg.305]

Vandamme, A.M., Bulens, R, Bemar, H., Nelles, L., Lijnen, R.H., and Collen, D., Construction and characterization of recombinant murine monoclonal antibody directed against human fibrin fragment-D dimer, Eur. ]. Biochem., 192, 767-775, 1990. [Pg.582]

Figure 26. Reconstruction of the tunica intima on the inner surface of a clinically used polyethylene terephtalate vascular prosthesis. A non-modified inner surface of the prosthesis, B immobilization of defined assemblies of protein molecules (e.g., collagenfiarninin or collagen+fibrin) on the inner surface of the graft, C immunofluorescence of von Willebrand factor, a marker of the identity a differentiation of vascular endothelial cells, in human saphenous vein endothelial cells in cultures on the inner surface of a prosthesis coated with collagen and larninin, D detail of a layer of endothelial cells growing on a layer of collagen and fibrin. Note well developed talin-containing focal adhesion plaques. A, B conventional optical microscope, C, D confocal microscope Leica DM 2500 [30,31]. Figure 26. Reconstruction of the tunica intima on the inner surface of a clinically used polyethylene terephtalate vascular prosthesis. A non-modified inner surface of the prosthesis, B immobilization of defined assemblies of protein molecules (e.g., collagenfiarninin or collagen+fibrin) on the inner surface of the graft, C immunofluorescence of von Willebrand factor, a marker of the identity a differentiation of vascular endothelial cells, in human saphenous vein endothelial cells in cultures on the inner surface of a prosthesis coated with collagen and larninin, D detail of a layer of endothelial cells growing on a layer of collagen and fibrin. Note well developed talin-containing focal adhesion plaques. A, B conventional optical microscope, C, D confocal microscope Leica DM 2500 [30,31].
Exposure to high concentrations may cause tracheobronchitis and pulmonary edema. The irritation threshold in humans is 0.2 5-0.5 ppm, and concentrations above Ippm are extremely irritating to all mucous membranes within 5 minutes. Fatalities have been reported at levels as low as 10ppm, and 150 ppm was lethal after 10 minutes. The violent irritant effect usually prevents chronic toxicity in humans. Skin contact causes irritation, burns, and epidermal necrosis." Eye splashes cause corneal damage, palpebral edema, blepharoconjunctivitis, and fibrinous or purulent discharge. ... [Pg.23]


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See also in sourсe #XX -- [ Pg.92 ]




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