Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Fibrinogen representation

Figure 51-4. Diagrammatic representation (not to scaie) of fibrinogen showing pairs of Aa, B 3, and y chains iinked by disuifide bonds. (FPA, fibrinopeptide A FPB, fibrinopeptide B.)... Figure 51-4. Diagrammatic representation (not to scaie) of fibrinogen showing pairs of Aa, B 3, and y chains iinked by disuifide bonds. (FPA, fibrinopeptide A FPB, fibrinopeptide B.)...
Zhang. S. M. and Loker, E. S., Representation of an immune responsive gene family encoding fibrinogen-related proteins in the freshwater mollusk Biomphalaria glabrata, Gene, 341, 255, 2004. [Pg.380]

Figure 9.7. Diagrammatic representation of the fibrinogen molecule and its conversion to the soft clot of fibrin. Reproduced (in modified form) by permission from Textbook of Biochemistry with Clinical Correlations (3rd Ed.) Devlin (1992). This material is used by permission of John Wiley Sons, Inc. Figure 9.7. Diagrammatic representation of the fibrinogen molecule and its conversion to the soft clot of fibrin. Reproduced (in modified form) by permission from Textbook of Biochemistry with Clinical Correlations (3rd Ed.) Devlin (1992). This material is used by permission of John Wiley Sons, Inc.
Schematic representation of Subsite Utilization in Thrombin Complexes (after Reference 8). Fibrinogen interacts with three thrombin subsites (here thrombin is represented by a large oval and the interconnected subsites by an irregular three-armed shape). Physiological effectors of thrombin and thrombin inhibitors form distinct interactions at these subsites. Additional subsites, such as the heparin-binding site, exist on the thrombin surface and are not indicated here. Schematic representation of Subsite Utilization in Thrombin Complexes (after Reference 8). Fibrinogen interacts with three thrombin subsites (here thrombin is represented by a large oval and the interconnected subsites by an irregular three-armed shape). Physiological effectors of thrombin and thrombin inhibitors form distinct interactions at these subsites. Additional subsites, such as the heparin-binding site, exist on the thrombin surface and are not indicated here.
Schematic representation of the principal intermolecular interactions of a fibrinogen peptide A mimetic within the active site... Schematic representation of the principal intermolecular interactions of a fibrinogen peptide A mimetic within the active site...
Figure 10.38. Structure of a Fibrinogen Molecule. (A) A ribbon diagram. The two rod regions are a-helical coiled coils, connected to a globular region at each end. (B) A schematic representation showing the positions of the fibrinopeptides A and B. Figure 10.38. Structure of a Fibrinogen Molecule. (A) A ribbon diagram. The two rod regions are a-helical coiled coils, connected to a globular region at each end. (B) A schematic representation showing the positions of the fibrinopeptides A and B.
Figure 4 Schematic representation of the polymerization of fibrin and fibrinolysis. Fibrinogen molecules are soluble in the blood until thrombin cleaves the A fibrinopeptides, yielding desA fibrin monomer, which assemble in a half-staggered fashion to make two-stranded protofibrils. Factor Xllla rapidly crosslinks the adjacent y chains. The B fibrinopeptides are cleaved more slowly mosdy after polymerization begins. On cleavage of the B fibrinopeptides, the aC domains are released, bringing protofibrils together more efficiendy to produce thicker fibers. Factor Xllla crosslinks the a chains more slowly, to stabilize the clot more fully. Plasminogen is converted to plasmin by tissue plasminogen activator on the fibrin surface plasmin cleaves specific peptide bonds (arrows) to dissolve the clot. Figure 4 Schematic representation of the polymerization of fibrin and fibrinolysis. Fibrinogen molecules are soluble in the blood until thrombin cleaves the A fibrinopeptides, yielding desA fibrin monomer, which assemble in a half-staggered fashion to make two-stranded protofibrils. Factor Xllla rapidly crosslinks the adjacent y chains. The B fibrinopeptides are cleaved more slowly mosdy after polymerization begins. On cleavage of the B fibrinopeptides, the aC domains are released, bringing protofibrils together more efficiendy to produce thicker fibers. Factor Xllla crosslinks the a chains more slowly, to stabilize the clot more fully. Plasminogen is converted to plasmin by tissue plasminogen activator on the fibrin surface plasmin cleaves specific peptide bonds (arrows) to dissolve the clot.

See other pages where Fibrinogen representation is mentioned: [Pg.811]    [Pg.88]    [Pg.209]    [Pg.225]    [Pg.106]    [Pg.455]    [Pg.285]    [Pg.722]    [Pg.425]    [Pg.425]    [Pg.7]    [Pg.490]   
See also in sourсe #XX -- [ Pg.250 ]




SEARCH



Fibrinogen

© 2024 chempedia.info