Abstract
The experiments in this work were focused on determination of the extent to which fibrinogen component of fibrin glue (Hemaseel ™ HMN, Haemacure Biotech.) retained the conformation of the parent molecule after dry heat antiviral treatment (one hour at 100°C). For this purpose antigenic structure of the fibrinogen component, heated and non-heated, was compared to that of control fibrinogens, ie. the isolated one and the fibrinogen present in fresh human blood plasma. The analytic parameters CI 50 and CI S were calculated from the competitive inhibition data obtained in ELISA systems using antisera to fibrinogen, plasmic fragments D and E, and to polypeptide chains Aα, Bβ, and γ. These immunochemical analyses indicated that there was a modified expression of some fibrinogen epitopes probably resulting from unfolding of the Aα chain and the better exposure of the E domain to the hydrated environment induced upon a heating procedure. Our data show that dry heat treatment of fibrinogen component is not associated with a significant overall conformational change of the molecule.
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