The effect of Factor XIII-induced crosslinking of fibrin on its subsequent lysis by plasmin has been further investigated due, in part, to conflicting reports in the literature on this issue. The test system used involved I labelled plasma fibrin clots and the release of the radiolabel to measure lysis rate. It was found that, while the fibrin γ-γ crosslinks do not affect the rate of fibrin lysis, the α chain crosslinkage has a significant effect. Indeed, the increased complexity of the α chain crosslinkage endows fibrin with increased resistance to lysis. I labelled fibrin clots containing fibrin with and without crosslinked α chains, allowed the preferential removal of the non-crosslinked material. Discrepancies were noted when measuring ...
and fibrin-inhibitor cross-links. Our flow model, which is sensitive to cross-link-ing, was used to ...
Reported evidence of a role in fibrinolysis by fibrinopeptide (Fp)B-dependent intermolecular fibrin ...
Human fibrinogen 1 is homodimeric with respect to its γ chains (`γA-γA\u27), whereas fibrinogen 2 mo...
textabstractThe inhibitory effect of coagulation factor XIII (FXIII) on fibrinolysis has been studie...
In spontaneous fibrinolysis of an a2-plasmin inhibitor-deficient plasma clot or tissue-type plasmino...
In the presence of plasma transglutaminase (factor XIIIa) fibrin first undergoes intermolecular cova...
Assumptions regarding the elaboration of plasma cross-linked fibrin degradation products (XLFbDPs) i...
Factor XIII is responsible for the cross-linking of fibrin γ-chains in the early stages of clot form...
AbstractWe investigated the origins of greater clot rigidity associated with FXIIIa-dependent cross-...
textabstractEssentials Factor XIIIa inhibits fibrinolysis by forming fibrin-fibrin and fibrin-inhibi...
The major covalently linked multimolecular D fragments found in plasmic digests of factor XHIa cross...
Background: Factor XIII is a 320 kDa tetramer, comprising two enzymatic A‐subunits and two carrier B...
Background: Activated factor XIII (FXIIIa), a transglutaminase, introduces fibrin-fibrin and fibrin-...
Factor XIII(a) [FXIII(a)] stabilizes clots and increases resistance to fibrinolysis and mechanical d...
Coagulation factor XIII (FXIII) is a protransglutaminase enzyme that is activated at the end of the ...
and fibrin-inhibitor cross-links. Our flow model, which is sensitive to cross-link-ing, was used to ...
Reported evidence of a role in fibrinolysis by fibrinopeptide (Fp)B-dependent intermolecular fibrin ...
Human fibrinogen 1 is homodimeric with respect to its γ chains (`γA-γA\u27), whereas fibrinogen 2 mo...
textabstractThe inhibitory effect of coagulation factor XIII (FXIII) on fibrinolysis has been studie...
In spontaneous fibrinolysis of an a2-plasmin inhibitor-deficient plasma clot or tissue-type plasmino...
In the presence of plasma transglutaminase (factor XIIIa) fibrin first undergoes intermolecular cova...
Assumptions regarding the elaboration of plasma cross-linked fibrin degradation products (XLFbDPs) i...
Factor XIII is responsible for the cross-linking of fibrin γ-chains in the early stages of clot form...
AbstractWe investigated the origins of greater clot rigidity associated with FXIIIa-dependent cross-...
textabstractEssentials Factor XIIIa inhibits fibrinolysis by forming fibrin-fibrin and fibrin-inhibi...
The major covalently linked multimolecular D fragments found in plasmic digests of factor XHIa cross...
Background: Factor XIII is a 320 kDa tetramer, comprising two enzymatic A‐subunits and two carrier B...
Background: Activated factor XIII (FXIIIa), a transglutaminase, introduces fibrin-fibrin and fibrin-...
Factor XIII(a) [FXIII(a)] stabilizes clots and increases resistance to fibrinolysis and mechanical d...
Coagulation factor XIII (FXIII) is a protransglutaminase enzyme that is activated at the end of the ...
and fibrin-inhibitor cross-links. Our flow model, which is sensitive to cross-link-ing, was used to ...
Reported evidence of a role in fibrinolysis by fibrinopeptide (Fp)B-dependent intermolecular fibrin ...
Human fibrinogen 1 is homodimeric with respect to its γ chains (`γA-γA\u27), whereas fibrinogen 2 mo...