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.
