Adsorption of Fibrinogen and Fragment D of Fibrinogen onto the Insolubilized αChain of Fibrin^[*]

Summary

After thrombin treatment insolubilized fibrinmonomer, which is obtained from insolubilized fibrinogen covalently bound to agarose, adsorbs soluble fibrin and its derivatives from solutions. The immobilized proteins are attached to the agarose by the ‘A’ αchain. After reduction of the disulfide bridges the β and γchains can be removed from the agarose.After thrombin treatment the immobilized αchain adsorbs fibrinogen and fragment D. To some extent the β and γchain do not seem necessary for the adsorption. The amount adsorbed increases, when thrombin treatment of the insolubilized protein follows the reduction process.This may indicate that the fibrinopeptides ‘A’ of the insolubilized αchain are better accessible after the removal of the β and γchains.

Presented at the workshop on “Shape and Structure of Fibrinogen” Martinsried, March 19,1977

• References

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