[Binding of alpha-2-antiplasmin with fibrinogen/fibrin and their fragments independent of factor XIII].
Possible interaction of alpha-2-antiplasmin with fibrinogen, fibrin and their fragments independent of factor XIII as well as the inhibitor effect on the Glu-plasminogen activation by tissue activator were studied. It was shown that alpha-2-antiplasmin is adsorbed on desAA- and desAABBfibrin films (Kd 69.0 +/- 1.0 nM 68.6 +/- 5.3 nM, respectively). Glu-Plasminogen has no effect on the inhibitor binding with desAABBfibrin. Alpha-2-antiplasmin shows strong affinity for fibrin D-dimer (Kd 65.0 +/- 4.0 nM) and D-fragment of fibrinogen (Kd 119.0 +/- 21.0 nM), but it does not interact with E-fragment. The inhibitor inside the fibrin clot decreases 10 times the activation rate of Glu-plasminogen by the tissue activator both is the presence and without factor XIII at physiological ratio of Glu-plasminogen, tissue activator, fibrin and alpha-2-antiplasmin. Thus we have shown that fibrinogen/fibrin binds alpha-2-antiplasmin independent of the factor XIII. Binding sites of the inhibitor are localized in D-fragment of fibrinogen and/or fibrin D-dimer. Alpha-2-antiplasmin inhibits the Glu-plasminogen activation by tissue activator on fibrin.
Zadorozhna
M B
MB
Hrynenko
T V
TV
Iusova
O I
OI
Volkov
H L
HL
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D005169:Factor VIII / Q000737:chemistry*; D005337:Fibrin / Q000737:chemistry*; D005340:Fibrinogen / Q000737:chemistry*; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry*; D013053:Spectrophotometry; D010959:Tissue Plasminogen Activator / Q000494:pharmacology; D000979:alpha-2-Antiplasmin / Q000737:chemistry*
D010446:Peptide Fragments; D000979:alpha-2-Antiplasmin; D005169:Factor VIII; D005337:Fibrin; D005340:Fibrinogen; D010959:Tissue Plasminogen Activator