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Thromb Haemost 1979; 41(04): 687-690
DOI: 10.1055/s-0038-1646826
Original Articles
Schattauer GmbH Stuttgart

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

F R Matthias
The Department of Medicine, Justus Liebig University, Giessen, West-Germany
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Publication History

Publication Date:
09 July 2018 (online)

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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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