[Plasminogen-binding centers of molecules of fibrinogen, fibrin and products of their proteolysis].
Using affinity chromatography, the binding of Lys-plasminogen to fibrinogen, fibrin and the consecutively formed products of their proteolysis was studied. The optimal conditions for this binding were elaborated, and the quantitative parameters of Lys-plasminogen binding to fibrinogen-Sepharose were determined. It was found that the interaction of Lys-plasminogen with fibrinogen- and fibrin-Sepharose is provided for by the lysine-binding sites of the proenzyme molecule. After partial hydrolysis of fibrinogen by plasmin, the amount of adsorbed plasminogen increases and the type of binding changes; part of the proenzyme molecules bind in the presence of 0.003 M 6-aminohexanoic acid, i.e., when lysine-binding sites appear to be blocked. A comparative study of plasminogen binding to fibrinogen fragments was carried out. The resistance of the complexes formed to the effect of 6-aminohexanoic acid and arginine competing for the binding sites was determined. The data obtained testify to the appearance of additional plasminogen-binding sites in the fibrinogen molecule during proteolysis. These sites are complementary for both lysine-and arginine-binding sites of the plasminogen molecule and are localized in the peripheral domains of the fibrinogen molecule.
Grinenko
T V
TV
Tret'iachenko
V G
VG
Kudinov
S A
SA
Medved'
L V
LV
D001665:Binding Sites; D002846:Chromatography, Affinity; D005337:Fibrin / Q000378:metabolism*; D005338:Fibrin Fibrinogen Degradation Products / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D005342:Fibrinolysis; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D010446:Peptide Fragments / Q000378:metabolism*; D010958:Plasminogen / Q000378:metabolism*
D005338:Fibrin Fibrinogen Degradation Products; D010446:Peptide Fragments; C018998:lysyl-plasminogen; D005337:Fibrin; D005340:Fibrinogen; D010958:Plasminogen
Plazminogensviazyvaiushchie tsentry molekuly fibrinogena, fibrina i produktov ikh proteoliza.