Fractionation of plasmic fibrin(ogen) digests by lectin affinity chromatography.

A method for the fractionation of plasmic digests of both fibrinogen and fibrin was developed by taking advantage of the different chromatographic behaviour of fibrinogen and its fragments on immobilized concanavalin A and Lens culinaris agglutinin. Columns with different lectin concentration but with the same total lectin content were tested. Fragment E was retained on all the concanavalin A-Sepharose preparations while fragment D was mostly eluted in the unbound fraction. However, the binding of fragment DD depended on the lectin concentration of the gel. Thus, the percentage of fragment DD specifically bound to concanavalin A-Sepharose increased from 5-10% to 67% as the lectin density of the gel increased from 0.9 to 8.7 mg/ml gel. On the other hand, Lens culinaris agglutinin-Sepharose retained fibrinogen and high molecular weight fragments depending on the lectin concentration of the gel while neither fragment E nor fragment D were bound to any of the columns.