Biochemical study of adduct synthesis between fibrin monomers and elastin.
Monomers of fibrin generated by thrombin from fibrinogen reacted with elastin to give a new addition product or adduct. Adduct formation resulted from a covalent bond between fibrin monomers and elastin. The kinetic studies of this reaction confirmed that the adduct was formed before fibrin precipitated to produce the clot. The reaction depended on elastin, fibrinogen and thrombin concentrations. When thrombin-induced and reptilase-induced fibrin were compared, it became obvious that fibrin monomers did intervene more commonly as Des AA-fibrin than as Des AA.BB-fibrin. The adduct synthesis was completely inhibited by 150 microM of the peptide Gly-Pro-Arg-Pro which was previously known to stabilize the fibrin monomers and consequently to inhibit the polymerization completely. It is shown that FXIII could intervene directly in the reaction where homological quality of elastin (human versus bovine) and purity of thrombin were other important factors.
Martin
M T
MT
Unité 8 de Recherches de Cardiologie INSERM, Pessac, France.
Lefebvre
F
F
Rabaud
M
M
Graves
P V
PV
D000818:Animals; D012103:Batroxobin; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004549:Elastin; D005176:Factor XIII; D005338:Fibrin Fibrinogen Degradation Products; D005340:Fibrinogen; D006801:Humans; D007700:Kinetics; D013917:Thrombin
D005338:Fibrin Fibrinogen Degradation Products; C011468:fibrinmonomer; D005340:Fibrinogen; D004549:Elastin; D005176:Factor XIII; D012103:Batroxobin; D013917:Thrombin