Antigenic properties of fibrinogen component of Hemaseel HMN subjected to the antiviral severe dry heat treatment.
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 degrees C). For this purpose antigenic structure of the fibrinogen component, heated and non-heated, was compared to that of control fibrinogens, i.e. the isolated one and the fibrinogen present in fresh human blood plasma. The analytic parameters CI50 and CIs were calculated from the competitive inhibition data obtained in ELISA systems using antisera to fibrinogen, plasmic fragments D and E, and to polypeptide chains A alpha, B beta, and gamma. These immunochemical analyses indicated that there was a modified expression of some fibrinogen epitopes probably resulting from unfolding of the A alpha 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.
Cierniewski
C S
CS
Department of Biophysics, Medical University in Lodz, Poland.
Pluskota
E
E
Cieslak
M
M
Brodniewicz
T
T
Nowotarski
M
M
D000939:Epitopes / Q000737:chemistry / Q000276:immunology*; D015718:Fibrin Tissue Adhesive / Q000737:chemistry / Q000276:immunology*; D005340:Fibrinogen / Q000737:chemistry / Q000276:immunology*; D006358:Hot Temperature; D006801:Humans; D011487:Protein Conformation
D000939:Epitopes; D015718:Fibrin Tissue Adhesive; D005340:Fibrinogen