The binding of fibrin sealant to collagen is influenced by the method of purification and the cross-linked fibrinogen–fibronectin (heteronectin) content of the ‘fibrinogen’ component-Reference-Cited by-同舟云学术

The binding of fibrin sealant to collagen is influenced by the method of purification and the cross-linked fibrinogen–fibronectin (heteronectin) content of the ‘fibrinogen’ component

Published:2005-03 Issue:2 Volume:16 Page:111-117
ISSN:0957-5235
Container-title:Blood Coagulation & Fibrinolysis
language:en
Short-container-title:

Author:

Bar Lilliana,Malka Osnat,Naboichenko Elvira,Nur Israel

Publisher

Ovid Technologies (Wolters Kluwer Health)

Subject

Hematology,General Medicine

Reference7 articles.

1. The effect of FXIII and fibronectin on the viscoelasticity of fibrinogen surface layers;King;Thromb Res,1988

2. FXIII induced gelation of human fibrinogen – an alternative thiol enhanced, thrombin independent pathway;Blomback;Thromb Res,1985

3. Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin–fibrin matrix;Corbett;J Biol Chem,1997

4. Inhibition of blood coagulation factor XIIIa-mediated cross-linking between fibronectin and collagen by polyamines;Mosher;J Supramol Struct,1979

5. Rapid methods for isolation of human plasma fibronectin;Miekka;Thromb Res,1982

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