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

Two fibrinogen preparations, each an intermediate in the manufacture of the 'fibrinogen' component of a commercial human tissue sealant, were made from a common cryoprecipitate source. The first preparation, prepared according to the process described by Schwartz et al. had a higher ratio of clottable to total protein than the second preparation, prepared according to that by Martinowitz and Bal but a much lower ratio of fibronectin to fibrinogen. After clotting with thrombin and solubilization and reduction of the clots, sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a much higher content of high molecular weight polymers of fibrin(ogen) in the second preparation than in the first. The second preparation bound to collagen more strongly than did cryoprecipitate and much more strongly than did the first one. Experiments with highly purified proteins showed that fibronectin was essential in promoting progressive binding of fibrinogen to collagen under the action of activated factor XIII (transglutaminase). It was concluded that, because of their method of purification from cryoprecipitate, preparations of fibrinogen differ in their content of fibronectin and heteronectin. The binding of these proteins to collagen may improve the adhesion of tissue sealant clots to the extracellular matrix.