High Resolution Electrophoretic Analysis of Human Fibrinogen and Its Crosslinked Intermediates

Summary

Heterogeneity in human fibrinogen was examined using an improved two-dimensional isoelectric focusing-SDS polyacrylamide gel electrophoretic procedure. Four different preparations of fibrinogen were compared: single donor fibrinogen prepared from plasma by precipitation with ammonium sulfate or by affinity chromatography on fibrin-monomer Sepharose, fraction I—4 prepared from Cohn fraction I paste, and Kabi grade L. The subunit Aα, Bβ, and γ chains in all preparations had marked charge heterogeneity. The three chains were clearly separated from each other and a range of isoelectric points for each chain could be assigned. Minor variations in the subunit heterogeneity of the different preparations were found. Intermediates in the transition from fibrinogen to crosslinked fibrin were also examined. A striking increase in the heterogeneity of the α chain was observed during crosslinking.

Keywords

Fibrinogen - Fibrinogen heterogeneity - Two-dimensional electrophoresis - Crosslinking

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