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Human fibrinogens

In the flow cell, the test surfaces were exposed to the flowing solutions under well characterized flow conditions. Carbon, polystyrene, and polycarbonate surfaces were exposed to the flowing (135/sec. shear rate), dilute (100 micrograms/ml.) solutions of intact native human fibrinogen, human fibrinogen with the alpha chain... [Pg.54]

Fibrinogen (human) active substance supplied by CSL Behring for further manufacturing of fibrin sealant patch by Nycomed... [Pg.222]

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]

Components/ mechanism of action Human plasma, fibrinogen and thrombin, virally inactivated, hemostat, sealant. Autologous fibrinogen -t-platelet-rich plasma, hemostatic gel. Bovine collagen, bovine thrombin, plus autologous human plasma, hemostatic agent. Bovine collagen and bovine thrombin. Expands 20% which aids in hemostatic effect. [Pg.1106]

Mature human albumin consists of one polypeptide chain of 585 amino acids and contains 17 disulfide bonds. By the use of proteases, albumin can be subdivided into three domains, which have different functions. Albumin has an ellipsoidal shape, which means that it does not increase the viscosity of the plasma as much as an elongated molecule such as fibrinogen does. Because of its relatively low molecular mass (about 69 kDa) and high concentration, albumin is thought to be responsible for 75-80% of the osmotic pressure of human plasma. Electrophoretic smdies have shown that the plasma of certain humans lacks albumin. These subjects are said to exhibit analbuminemia. One cause of this condition is a mutation that affects spUcing. Subjects with analbuminemia show only moderate edema, despite the fact that albumin is the major determinant of plasma osmotic pressure. It is thought that the amounts of the other plasma proteins increase and compensate for the lack of albumin. [Pg.584]

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]

Kirschbaum, N. E. and Budzynski, A. Z., A unique proteolytic fragment of human fibrinogen containing the Aa COOH-terminal domain of the native molecule, J. Biol. Chem., 265, 13669, 1990. [Pg.285]


See other pages where Human fibrinogens is mentioned: [Pg.124]    [Pg.32]    [Pg.87]    [Pg.358]    [Pg.262]    [Pg.129]    [Pg.302]    [Pg.276]    [Pg.7]    [Pg.334]    [Pg.404]    [Pg.404]    [Pg.527]    [Pg.311]    [Pg.311]    [Pg.116]    [Pg.126]    [Pg.358]    [Pg.311]    [Pg.226]    [Pg.1636]    [Pg.471]    [Pg.124]    [Pg.32]    [Pg.87]    [Pg.358]    [Pg.262]    [Pg.129]    [Pg.302]    [Pg.276]    [Pg.7]    [Pg.334]    [Pg.404]    [Pg.404]    [Pg.527]    [Pg.311]    [Pg.311]    [Pg.116]    [Pg.126]    [Pg.358]    [Pg.311]    [Pg.226]    [Pg.1636]    [Pg.471]    [Pg.457]    [Pg.44]    [Pg.532]    [Pg.179]    [Pg.144]    [Pg.310]    [Pg.310]    [Pg.311]    [Pg.534]    [Pg.534]    [Pg.1113]    [Pg.1115]    [Pg.1116]    [Pg.1118]    [Pg.169]    [Pg.169]    [Pg.264]    [Pg.602]    [Pg.90]    [Pg.40]    [Pg.145]    [Pg.131]   
See also in sourсe #XX -- [ Pg.102 ]




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