Reduction of insolubilized fibrinogen

Insolubilization of fibrinogen is achieved by covalent fixation onto cyanogen bromide activated agarose. When insolubilized fibrinogen (FG-ag) is reduced in order to separate the fibrinogen molecule into its chains, disc-electrophoretic patterns reveal that the (‘A’) α-chains remain with the insolub...

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Veröffentlicht in:Thrombosis research 1974-06, Vol.4 (6), p.803-808
Hauptverfasser: Matthias, F.R., Heene, D.L., Wegrzynowicz, Z.
Format: Artikel
Sprache:eng
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Zusammenfassung:Insolubilization of fibrinogen is achieved by covalent fixation onto cyanogen bromide activated agarose. When insolubilized fibrinogen (FG-ag) is reduced in order to separate the fibrinogen molecule into its chains, disc-electrophoretic patterns reveal that the (‘A’) α-chains remain with the insoluble agarose whereas the (B) β-chains and the γ-chains appear in the supernatant. It is assumed that covalent fixation of fibrinogen to agarose almost exclusively takes place at the (‘A’) α-chain and that the (‘A’) α-chain is located at the surface of the fibrinogen molecule.
ISSN:0049-3848
1879-2472
DOI:10.1016/0049-3848(74)90023-1